Type 5 secretion system antigens as vaccines against Gram-negative bacterial infections.
Journal
NPJ vaccines
ISSN: 2059-0105
Titre abrégé: NPJ Vaccines
Pays: England
ID NLM: 101699863
Informations de publication
Date de publication:
01 Sep 2024
01 Sep 2024
Historique:
received:
13
02
2024
accepted:
14
08
2024
medline:
2
9
2024
pubmed:
2
9
2024
entrez:
1
9
2024
Statut:
epublish
Résumé
Infections caused by Gram-negative bacteria are leading causes of mortality worldwide. Due to the rise in antibiotic resistant strains, there is a desperate need for alternative strategies to control infections caused by these organisms. One such approach is the prevention of infection through vaccination. While live attenuated and heat-killed bacterial vaccines are effective, they can lead to adverse reactions. Newer vaccine technologies focus on utilizing polysaccharide or protein subunits for safer and more targeted vaccination approaches. One promising avenue in this regard is the use of proteins released by the Type 5 secretion system (T5SS). This system is the most prevalent secretion system in Gram-negative bacteria. These proteins are compelling vaccine candidates due to their demonstrated protective role in current licensed vaccines. Notably, Pertactin, FHA, and NadA are integral components of licensed vaccines designed to prevent infections caused by Bordetella pertussis or Neisseria meningitidis. In this review, we delve into the significance of incorporating T5SS proteins into licensed vaccines, their contributions to virulence, conserved structural motifs, and the protective immune responses elicited by these proteins.
Identifiants
pubmed: 39218947
doi: 10.1038/s41541-024-00953-6
pii: 10.1038/s41541-024-00953-6
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
159Informations de copyright
© 2024. The Author(s).
Références
WHO. List of bacteria for which new antibiotics are urgently needed (WHO News, 2019).
Murray, C. J. et al. Global burden of bacterial antimicrobial resistance in 2019: a systematic analysis. Lancet 399, 629–655 (2022).
doi: 10.1016/S0140-6736(21)02724-0
O’Neill, J. Tackling drug-resistant infections globally: final report and recommendations (Government of the United Kingdom, 2016).
Francis, M. J. Recent advances in vaccine technologies. Vet. Clin. North Am. Small Anim. Pract. 48, 231 (2018).
pubmed: 29217317
doi: 10.1016/j.cvsm.2017.10.002
Jansen, K. U. & Anderson, A. S. The role of vaccines in fighting antimicrobial resistance (AMR). Hum. Vaccin Immunother. 14, 2142–2149 (2018).
pubmed: 29787323
pmcid: 6183139
doi: 10.1080/21645515.2018.1476814
WHO. Reported cases of vaccine prevenatble diseases (WHO, 2019).
Plotkin, S. A. Correlates of protection induced by vaccination. Clin. Vaccin. Immunol. 17, 1055–1065 (2010).
doi: 10.1128/CVI.00131-10
Pollard, A. J. & Bijker, E. M. & Publisher Correction: A guide to vaccinology: from basic principles to new developments. Nat. Rev. Immunol. 21, 129 (2021).
pubmed: 33402728
pmcid: 8095270
doi: 10.1038/s41577-020-00497-5
Poolman, J. T. Expanding the role of bacterial vaccines into life-course vaccination strategies and prevention of antimicrobial-resistant infections. NPJ Vaccines 5, 84 (2020).
pubmed: 32963814
pmcid: 7486369
doi: 10.1038/s41541-020-00232-0
Clem, A. S. Fundamentals of vaccine immunology. J. Glob. Infect. Dis. 3, 73–78 (2011).
pubmed: 21572612
pmcid: 3068582
doi: 10.4103/0974-777X.77299
Golubovskaya, V. & Wu, L. Different subsets of T cells, memory, effector functions, and CAR-T immunotherapy. Cancers 8, https://doi.org/10.3390/cancers8030036 (2016).
Romagnani, S. Th1/Th2 cells. Inflamm. Bowel Dis. 5, 285–294 (1999).
pubmed: 10579123
doi: 10.1097/00054725-199911000-00009
Rivera-Hernandez, T. et al. Vaccine-induced Th1-type response protects against invasive Group A Streptococcus infection in the absence of opsonizing antibodies. mBio 11, https://doi.org/10.1128/mBio.00122-20 (2020).
Crotty, S. T follicular helper cell differentiation, function, and roles in disease. Immunity 41, 529–542 (2014).
pubmed: 25367570
pmcid: 4223692
doi: 10.1016/j.immuni.2014.10.004
Schroeder, H. W. Jr & Cavacini, L. Structure and function of immunoglobulins. J. Allergy Clin. Immunol. 125, S41–S52 (2010).
pubmed: 20176268
pmcid: 3670108
doi: 10.1016/j.jaci.2009.09.046
Sharp, T. H. et al. Insights into IgM-mediated complement activation based on in situ structures of IgM-C1-C4b. Proc. Natl Acad. Sci. 116, 11900–11905 (2019).
pubmed: 31147461
pmcid: 6575175
doi: 10.1073/pnas.1901841116
Alugupalli, A. S. et al. The lack of natural IgM increases susceptibility and impairs anti-Vi polysaccharide IgG responses in a mouse model of typhoid. Immunohorizons 6, 807–816 (2022).
pubmed: 36480484
doi: 10.4049/immunohorizons.2200088
Gil-Cruz, C. et al. The porin OmpD from nontyphoidal Salmonella is a key target for a protective B1b cell antibody response. Proc. Natl Acad. Sci. USA 106, 9803–9808 (2009).
pubmed: 19487686
pmcid: 2701014
doi: 10.1073/pnas.0812431106
Vidarsson, G., Dekkers, G. & Rispens, T. IgG subclasses and allotypes: from structure to effector functions. Front. Immunol. 5, 520 (2014).
pubmed: 25368619
pmcid: 4202688
doi: 10.3389/fimmu.2014.00520
Dangl, J. L. et al. Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies. EMBO J. 7, 1989–1994 (1988).
pubmed: 3138110
pmcid: 454472
doi: 10.1002/j.1460-2075.1988.tb03037.x
Goh, Y. S. et al. Human IgG isotypes and activating Fcγ receptors in the interaction of Salmonella enterica serovar Typhimurium with phagocytic cells. Immunology 133, 74–83 (2011).
pubmed: 21323662
pmcid: 3088969
doi: 10.1111/j.1365-2567.2011.03411.x
Maguire, G. A., Kumararatne, D. S. & Joyce, H. J. Are there any clinical indications for measuring IgG subclasses? Ann. Clin. Biochem. 39, 374–377 (2002).
pubmed: 12117441
doi: 10.1258/000456302760042678
Kuijpers, T. W., Weening, R. S. & Out, T. A. IgG subclass deficiencies and recurrent pyogenic infections, unresponsiveness against bacterial polysaccharide antigens. Allergol. Immunopathol. 20, 28–34 (1992).
Vidarsson, G. et al. Isotypes and opsonophagocytosis of pneumococcus type 6B antibodies elicited in infants and adults by an experimental pneumococcus type 6B-tetanus toxoid vaccine. Infect. Immun. 66, 2866–2870 (1998).
pubmed: 9596761
pmcid: 108283
doi: 10.1128/IAI.66.6.2866-2870.1998
James, L. K. & Till, S. J. Potential mechanisms for IgG4 inhibition of immediate hypersensitivity reactions. Curr. Allergy Asthma Rep. 16, 23 (2016).
pubmed: 26892721
pmcid: 4759210
doi: 10.1007/s11882-016-0600-2
French, M. A. & Harrison, G. An investigation into the effect of the IgG antibody system on the susceptibility of IgA-deficient patients to respiratory tract infections. Clin. Exp. Immunol. 66, 640–647 (1986).
pubmed: 3568451
pmcid: 1542474
Wells, T. J. et al. Increased severity of respiratory infections associated with elevated anti-LPS IgG2 which inhibits serum bactericidal killing. J. Exp. Med. 211, 1893–1904 (2014).
pubmed: 25113975
pmcid: 4144740
doi: 10.1084/jem.20132444
Bianchi, A., Fantoni, S. & Prugnola, A. Meningococcal B vaccine and the vision of a meningitis free world. J. Prev. Med Hyg. 56, E140–E143 (2015).
pubmed: 26788735
pmcid: 4755123
Nix, E. B. et al. Risk of invasive Haemophilus influenzae type b (Hib) disease in adults with secondary immunodeficiency in the post-Hib vaccine era. Clin. Vaccin. Immunol. 19, 766–771 (2012).
doi: 10.1128/CVI.05675-11
Domínguez-Medina, C. C. et al. Outer membrane protein size and LPS O-antigen define protective antibody targeting to the Salmonella surface. Nat. Commun. 11, 851 (2020).
pubmed: 32051408
pmcid: 7015928
doi: 10.1038/s41467-020-14655-9
MacLennan, C. A. et al. Dysregulated humoral immunity to nontyphoidal Salmonella in HIV-infected African adults. Science 328, 508–512 (2010).
pubmed: 20413503
pmcid: 3772309
doi: 10.1126/science.1180346
Coggon, C. F. et al. A novel method of serum resistance by Escherichia coli that causes urosepsis. mBio 9, https://doi.org/10.1128/mBio.00920-18 (2018).
Döring, G., Meisner, C. & Stern, M. A double-blind randomized placebo-controlled phase III study of a Pseudomonas aeruginosa flagella vaccine in cystic fibrosis patients. Proc. Natl Acad. Sci. USA 104, 11020–11025 (2007).
pubmed: 17585011
pmcid: 1904125
doi: 10.1073/pnas.0702403104
Chen, W. H. et al. Single-dose live oral cholera vaccine CVD 103-HgR protects against human experimental infection with Vibrio cholerae O1 El Tor. Clin. Infect. Dis. 62, 1329–1335 (2016).
pubmed: 27001804
pmcid: 4872293
doi: 10.1093/cid/ciw145
Tennant, S. M. & Levine, M. M. Live attenuated vaccines for invasive Salmonella infections. Vaccine 33, C36–C41 (2015).
pubmed: 25902362
pmcid: 4469493
doi: 10.1016/j.vaccine.2015.04.029
Taylor, D. N. et al. Evaluation of a bivalent (CVD 103-HgR/CVD 111) live oral cholera vaccine in adult volunteers from the United States and Peru. Infect. Immun. 65, 3852–3856 (1997).
pubmed: 9284163
pmcid: 175550
doi: 10.1128/iai.65.9.3852-3856.1997
Frey, J. Biological safety concepts of genetically modified live bacterial vaccines. Vaccine 25, 5598–5605 (2007).
pubmed: 17239999
doi: 10.1016/j.vaccine.2006.11.058
Crump, J. A. & Mintz, E. D. Global trends in typhoid and paratyphoid fever. Clin. Infect. Dis. 50, 241–246 (2010).
pubmed: 20014951
doi: 10.1086/649541
Fraser, A., Paul, M., Goldberg, E., Acosta, C. J. & Leibovici, L. Typhoid fever vaccines: systematic review and meta-analysis of randomised controlled trials. Vaccine 25, 7848–7857 (2007).
pubmed: 17928109
doi: 10.1016/j.vaccine.2007.08.027
Engels, E. A., Falagas, M. E., Lau, J. & Bennish, M. L. Typhoid fever vaccines: a meta-analysis of studies on efficacy and toxicity. BMJ 316, 110–116 (1998).
pubmed: 9462316
pmcid: 2665386
doi: 10.1136/bmj.316.7125.110
Ryan, M. et al. Distinct T-cell subtypes induced with whole cell and acellular pertussis vaccines in children. Immunology 93, 1–10 (1998).
pubmed: 9536112
pmcid: 1364099
doi: 10.1046/j.1365-2567.1998.00401.x
Jefferson, T., Rudin, M. & DiPietrantonj, C. Systematic review of the effects of pertussis vaccines in children. Vaccine 21, 2003–2014 (2003).
pubmed: 12706690
doi: 10.1016/S0264-410X(02)00770-3
van der Lee, S., Hendrikx, L. H., Sanders, E. A. M., Berbers, G. A. M. & Buisman, A. M. Whole-cell or acellular pertussis primary immunizations in infancy determines adolescent cellular immune profiles. Front. Immunol. 9, 51 (2018).
pubmed: 29416544
pmcid: 5787539
doi: 10.3389/fimmu.2018.00051
Muloiwa, R., Kagina, B. M., Engel, M. E. & Hussey, G. D. The burden of pertussis in low- and middle-income countries since the inception of the Expanded Programme on Immunization (EPI) in 1974: a systematic review protocol. Syst. Rev. 4, 62 (2015).
pubmed: 25930111
pmcid: 4419482
doi: 10.1186/s13643-015-0053-z
Cress, B. F. et al. Masquerading microbial pathogens: capsular polysaccharides mimic host-tissue molecules. FEMS Microbiol. Rev. 38, 660–697 (2014).
pubmed: 24372337
doi: 10.1111/1574-6976.12056
Horwitz, M. A. & Silverstein, S. C. Influence of the Escherichia coli capsule on complement fixation and on phagocytosis and killing by human phagocytes. J. Clin. Invest. 65, 82–94 (1980).
pubmed: 6985617
pmcid: 371342
doi: 10.1172/JCI109663
MacLennan, C. A., Martin, L. B. & Micoli, F. Vaccines against invasive Salmonella disease: current status and future directions. Hum. Vaccin. Immunother. 10, 1478–1493 (2014).
pubmed: 24804797
pmcid: 4185946
doi: 10.4161/hv.29054
Prinz, D. M., Smithson, S. L., Kieber-Emmons, T. & Westerink, M. A. Induction of a protective capsular polysaccharide antibody response to a multiepitope DNA vaccine encoding a peptide mimic of meningococcal serogroup C capsular polysaccharide. Immunology 110, 242–249 (2003).
pubmed: 14511238
pmcid: 1783044
doi: 10.1046/j.1365-2567.2003.01732.x
Ada, G. & Isaacs, D. Carbohydrate-protein conjugate vaccines. Clin. Microbiol. Infect. 9, 79–85 (2003).
pubmed: 12588327
doi: 10.1046/j.1469-0691.2003.00530.x
Buchwald, U. K. et al. Sequential administration of Prevnar 13™ and PNEUMOVAX™ 23 in healthy participants 50 years of age and older. Hum. Vaccin. Immunother. 17, 2678–2690 (2021).
pubmed: 34019468
pmcid: 8475587
doi: 10.1080/21645515.2021.1888621
Jossi, S. E. et al. Vi polysaccharide and conjugated vaccines afford similar early, IgM or IgG-independent control of infection but boosting with conjugated Vi vaccines sustains the efficacy of immune responses. Front. Immunol. 14, 1139329 (2023).
pubmed: 37033932
pmcid: 10076549
doi: 10.3389/fimmu.2023.1139329
Chen, D. J. et al. Delivery of foreign antigens by engineered outer membrane vesicle vaccines. Proc. Natl Acad. Sci. USA 107, 3099–3104 (2010).
pubmed: 20133740
pmcid: 2840271
doi: 10.1073/pnas.0805532107
van der Pol, L., Stork, M. & van der Ley, P. Outer membrane vesicles as platform vaccine technology. Biotechnol. J. 10, 1689–1706 (2015).
pubmed: 26912077
pmcid: 4768646
doi: 10.1002/biot.201400395
Beernink, P. T., Vianzon, V., Lewis, L. A., Moe, G. R. & Granoff, D. M. A Meningococcal outer membrane vesicle vaccine with overexpressed mutant fHbp elicits higher protective antibody responses in infant rhesus macaques than a licensed serogroup B vaccine. mBio 10, https://doi.org/10.1128/mBio.01231-19 (2019).
Sierra, G. V. et al. Vaccine against group B Neisseria meningitidis: protection trial and mass vaccination results in Cuba. NIPH Ann. 14, 195–207 (1991).
pubmed: 1812432
de Moraes, J. C. et al. Protective efficacy of a serogroup B meningococcal vaccine in Sao Paulo, Brazil. Lancet 340, 1074–1078 (1992).
pubmed: 1357461
doi: 10.1016/0140-6736(92)93086-3
Bjune, G. et al. Effect of outer membrane vesicle vaccine against group B meningococcal disease in Norway. Lancet 338, 1093–1096 (1991).
pubmed: 1682541
doi: 10.1016/0140-6736(91)91961-S
Kelly, C., Arnold, R., Galloway, Y. & O’Hallahan, J. A prospective study of the effectiveness of the New Zealand meningococcal B vaccine. Am. J. Epidemiol. 166, 817–823 (2007).
pubmed: 17615088
doi: 10.1093/aje/kwm147
Holst, J. et al. Vaccines against meningococcal serogroup B disease containing outer membrane vesicles (OMV): lessons from past programs and implications for the future. Hum. Vaccin Immunother. 9, 1241–1253 (2013).
pubmed: 23857274
pmcid: 3901813
doi: 10.4161/hv.24129
Serruto, D., Bottomley, M. J., Ram, S., Giuliani, M. M. & Rappuoli, R. The new multicomponent vaccine against meningococcal serogroup B, 4CMenB: immunological, functional and structural characterization of the antigens. Vaccine 30, B87–B97 (2012).
pubmed: 22607904
doi: 10.1016/j.vaccine.2012.01.033
Wedege, E. et al. Functional and specific antibody responses in adult volunteers in new zealand who were given one of two different meningococcal serogroup B outer membrane vesicle vaccines. Clin. Vaccin. Immunol. 14, 830–838 (2007).
doi: 10.1128/CVI.00039-07
Bottero, D. et al. Characterization of the immune response induced by pertussis OMVs-based vaccine. Vaccine 34, 3303–3309 (2016).
pubmed: 27151884
doi: 10.1016/j.vaccine.2016.04.079
Baker, J. L., Chen, L., Rosenthal, J. A., Putnam, D. & DeLisa, M. P. Microbial biosynthesis of designer outer membrane vesicles. Curr. Opin. Biotechnol. 29, 76–84 (2014).
pubmed: 24667098
doi: 10.1016/j.copbio.2014.02.018
Kim, S. H. et al. Structural modifications of outer membrane vesicles to refine them as vaccine delivery vehicles. Biochim. Biophys. Acta 1788, 2150–2159 (2009).
pubmed: 19695218
pmcid: 5007125
doi: 10.1016/j.bbamem.2009.08.001
Pastor, Y. et al. Towards a subunit vaccine from a Shigella flexneri ΔtolR mutant. Vaccine 36, 7509–7519 (2018).
pubmed: 30420041
doi: 10.1016/j.vaccine.2018.10.066
Liu, Q. et al. Outer membrane vesicles from flagellin-deficient Salmonella enterica serovar Typhimurium induce cross-reactive immunity and provide cross-protection against heterologous Salmonella challenge. Sci. Rep. 6, 34776 (2016).
pubmed: 27698383
pmcid: 5048178
doi: 10.1038/srep34776
Liu, Q. et al. Outer membrane vesicles derived from Salmonella Typhimurium mutants with truncated LPS induce cross-protective immune responses against infection of Salmonella enterica serovars in the mouse model. Int. J. Med. Microbiol. 306, 697–706 (2016).
pubmed: 27578609
pmcid: 5206754
doi: 10.1016/j.ijmm.2016.08.004
Gerke, C. et al. Production of a Shigella sonnei vaccine based on generalized modules for membrane antigens (GMMA), 1790GAHB. PLoS One 10, e0134478 (2015).
pubmed: 26248044
pmcid: 4527750
doi: 10.1371/journal.pone.0134478
Ausiello, C. M. et al. Acellular vaccines induce cell-mediated immunity to Bordetella pertussis antigens in infants undergoing primary vaccination against pertussis. Dev. Biol. Stand 89, 315–320 (1997).
pubmed: 9272365
Hodges, F. J., Von Vergel, L. T., Cunningham, A. F., Henderson, I. R. & Icke, C. Redefining the bacterial Type I protein secretion system. Adv. Microb. Physiol. 82, 155–204 (2023).
pubmed: 36948654
doi: 10.1016/bs.ampbs.2022.10.003
Costa, T. R. et al. Secretion systems in Gram-negative bacteria: structural and mechanistic insights. Nat. Rev. Microbiol. 13, 343–359 (2015).
pubmed: 25978706
doi: 10.1038/nrmicro3456
Christie, P. J. The rich tapestry of bacterial protein translocation systems. Protein J. 38, 389–408 (2019).
pubmed: 31407127
pmcid: 6826261
doi: 10.1007/s10930-019-09862-3
Palmer, T., Finney, A. J., Saha, C. K., Atkinson, G. C. & Sargent, F. A holin/peptidoglycan hydrolase-dependent protein secretion system. Mol. Microbiol. 115, 345–355 (2021).
pubmed: 32885520
doi: 10.1111/mmi.14599
Grossman, A. S., Mauer, T. J., Forest, K. T. & Goodrich-Blair, H. A widespread bacterial secretion system with diverse substrates. mBio 12, e0195621 (2021).
pubmed: 34399622
doi: 10.1128/mBio.01956-21
Dewan, K. K., Linz, B., DeRocco, S. E. & Harvill, E. T. Acellular pertussis vaccine components: today and tomorrow. Vaccines 8, https://doi.org/10.3390/vaccines8020217 (2020).
Gorringe, A. R. & Pajón, R. Bexsero: a multicomponent vaccine for prevention of meningococcal disease. Hum. Vaccines Immunotherapeutics 8, 174–183 (2012).
doi: 10.4161/hv.18500
Henderson, I. R., Navarro-Garcia, F., Desvaux, M., Fernandez, R. C. & Ala’Aldeen, D. Type V protein secretion pathway: the autotransporter story. Microbiol. Mol. Biol. Rev. 68, 692–744 (2004).
pubmed: 15590781
pmcid: 539010
doi: 10.1128/MMBR.68.4.692-744.2004
Meuskens, I., Saragliadis, A., Leo, J. C. & Linke, D. Type V secretion systems: an overview of passenger domain functions. Front. Microbiol 10, 1163 (2019).
pubmed: 31214135
pmcid: 6555100
doi: 10.3389/fmicb.2019.01163
Desvaux, M., Parham, N. J. & Henderson, I. R. The autotransporter secretion system. Res. Microbiol. 155, 53–60 (2004).
pubmed: 14990256
doi: 10.1016/j.resmic.2003.10.002
Henderson, I. R. et al. Renaming protein secretion in the gram-negative bacteria. Trends Microbiol. 8, 352 (2000).
pubmed: 11041650
doi: 10.1016/S0966-842X(00)01814-X
Leo, J. C., Grin, I. & Linke, D. Type V secretion: mechanism (s) of autotransport through the bacterial outer membrane. Philos. Trans. R. Soc. B Biol. Sci. 367, 1088–1101 (2012).
doi: 10.1098/rstb.2011.0208
Henderson, I. R., Navarro-Garcia, F. & Nataro, J. P. The great escape: structure and function of the autotransporter proteins. Trends Microbiol. 6, 370–378 (1998).
pubmed: 9778731
doi: 10.1016/S0966-842X(98)01318-3
Comanducci, M. et al. NadA, a novel vaccine candidate of Neisseria meningitidis. J. Exp. Med. 195, 1445–1454 (2002).
pubmed: 12045242
pmcid: 2193550
doi: 10.1084/jem.20020407
Gustafsson, L., Hallander, H. O., Olin, P., Reizenstein, E. & Storsaeter, J. A controlled trial of a two-component acellular, a five-component acellular, and a whole-cell pertussis vaccine. N. Engl. J. Med. 334, 349–356 (1996).
pubmed: 8538705
doi: 10.1056/NEJM199602083340602
Inatsuka, C. S. et al. Pertactin is required for Bordetella species to resist neutrophil-mediated clearance. Infect. Immun. 78, 2901–2909 (2010).
pubmed: 20421378
pmcid: 2897405
doi: 10.1128/IAI.00188-10
De Gouw, D., Diavatopoulos, D. A., Bootsma, H. J., Hermans, P. W. & Mooi, F. R. Pertussis: a matter of immune modulation. FEMS Microbiol. Rev. 35, 441–474 (2011).
pubmed: 21204863
doi: 10.1111/j.1574-6976.2010.00257.x
Hegerle, N. & Guiso, N. Antibody-mediated inhibition of Bordetella pertussis adenylate cyclase–haemolysin-induced macrophage cytotoxicity is influenced by variations in the bacterial population. Microbiology 160, 962–969 (2014).
pubmed: 24554758
doi: 10.1099/mic.0.074690-0
Edwards, K. M. et al. Adult immunization with acellular pertussis vaccine. JAMA 269, 53–56 (1993).
pubmed: 8416406
doi: 10.1001/jama.1993.03500010063032
Podda, A. et al. Comparative study of a whole-cell pertussis vaccine and a recombinant acellular pertussis vaccine. The Italian Multicenter Group for the Study of Recombinant Acellular Pertussis Vaccine. J. Pediatr. 124, 921–926 (1994).
pubmed: 8201477
doi: 10.1016/S0022-3476(05)83181-6
Cotter, P. A. et al. Filamentous hemagglutinin of Bordetella bronchiseptica is required for efficient establishment of tracheal colonization. Infect. Immun. 66, 5921–5929 (1998).
pubmed: 9826374
pmcid: 108750
doi: 10.1128/IAI.66.12.5921-5929.1998
Leininger, E. et al. Pertactin, an Arg-Gly-Asp-containing Bordetella pertussis surface protein that promotes adherence of mammalian cells. Proc. Natl Acad. Sci. USA 88, 345–349 (1991).
pubmed: 1988935
pmcid: 50807
doi: 10.1073/pnas.88.2.345
Scheller, E. V. & Cotter, P. A. Bordetella filamentous hemagglutinin and fimbriae: critical adhesins with unrealized vaccine potential. Pathog. Dis. 73, ftv079 (2015).
pubmed: 26416077
pmcid: 4626604
doi: 10.1093/femspd/ftv079
Shahin, R. D., Brennan, M. J., Li, Z. M., Meade, B. D. & Manclark, C. R. Characterization of the protective capacity and immunogenicity of the 69-kD outer membrane protein of Bordetella pertussis. J. Exp. Med. 171, 63–73 (1990).
pubmed: 2295882
doi: 10.1084/jem.171.1.63
Olin, P., Rasmussen, F., Gustafsson, L., Hallander, H. O. & Heijbel, H. Randomised controlled trial of two-component, three-component, and five-component acellular pertussis vaccines compared with whole-cell pertussis vaccine. Ad Hoc Group for the Study of Pertussis Vaccines. Lancet 350, 1569–1577 (1997).
pubmed: 9393335
doi: 10.1016/S0140-6736(97)06508-2
Di Tommaso, A. et al. Identification of subregions of Bordetella pertussis filamentous hemagglutinin that stimulate human T-cell responses. Infect. Immun. 59, 3313–3315 (1991).
pubmed: 1715327
pmcid: 258172
doi: 10.1128/iai.59.9.3313-3315.1991
King, A. J. et al. Role of the polymorphic region 1 of the Bordetella pertussis protein pertactin in immunity. Microbiology 147, 2885–2895 (2001).
pubmed: 11700340
doi: 10.1099/00221287-147-11-2885
Rodríguez, M. E., Hellwig, S. M., Pérez Vidakovics, M. L., Berbers, G. A. & van de Winkel, J. G. Bordetella pertussis attachment to respiratory epithelial cells can be impaired by fimbriae-specific antibodies. FEMS Immunol. Med. Microbiol. 46, 39–47 (2006).
pubmed: 16420595
doi: 10.1111/j.1574-695X.2005.00001.x
Berggård, K., Lindahl, G., Dahlbäck, B. & Blom, A. M. Bordetella pertussis binds to human C4b-binding protein (C4BP) at a site similar to that used by the natural ligand C4b. Eur. J. Immunol. 31, 2771–2780 (2001).
pubmed: 11536176
doi: 10.1002/1521-4141(200109)31:9<2771::AID-IMMU2771>3.0.CO;2-0
Charles, I. et al. Expression of the Bordetella pertussis P.69 pertactin adhesin in Escherichia coli: fate of the carboxy-terminal domain. Microbiology 140, 3301–3308 (1994).
pubmed: 7881548
doi: 10.1099/13500872-140-12-3301
Everest, P. et al. Role of the Bordetella pertussis P.69/pertactin protein and the P.69/pertactin RGD motif in the adherence to and invasion of mammalian cells. Microbiology 142, 3261–3268 (1996).
pubmed: 8969522
doi: 10.1099/13500872-142-11-3261
Storsaeter, J., Hallander, H. O., Gustafsson, L. & Olin, P. Levels of anti-pertussis antibodies related to protection after household exposure to Bordetella pertussis. Vaccine 16, 1907–1916 (1998).
pubmed: 9796042
doi: 10.1016/S0264-410X(98)00227-8
Hijnen, M. et al. Epitope structure of the Bordetella pertussis protein P.69 pertactin, a major vaccine component and protective antigen. Infect. Immun. 72, 3716–3723 (2004).
pubmed: 15213111
pmcid: 427433
doi: 10.1128/IAI.72.7.3716-3723.2004
Lesne, E. et al. Acellular pertussis vaccines induce anti-pertactin bactericidal antibodies which drives the emergence of Pertactin-negative strains. Front. Microbiol 11, 2108 (2020).
pubmed: 32983069
pmcid: 7481377
doi: 10.3389/fmicb.2020.02108
Hellwig, S. M., Rodriguez, M. E., Berbers, G. A., van de Winkel, J. G. & Mooi, F. R. Crucial role of antibodies to pertactin in Bordetella pertussis immunity. J. Infect. Dis. 188, 738–742 (2003).
pubmed: 12934190
doi: 10.1086/377283
Weiss, A. A., Mobberley, P. S., Fernandez, R. C. & Mink, C. M. Characterization of human bactericidal antibodies to Bordetella pertussis. Infect. Immun. 67, 1424–1431 (1999).
pubmed: 10024590
pmcid: 96476
doi: 10.1128/IAI.67.3.1424-1431.1999
Jongerius, I., Schuijt, T. J., Mooi, F. R. & Pinelli, E. Complement evasion by Bordetella pertussis: implications for improving current vaccines. J. Mol. Med. 93, 395–402 (2015).
pubmed: 25686752
doi: 10.1007/s00109-015-1259-1
Marzouqi, I., Richmond, P., Fry, S., Wetherall, J. & Mukkur, T. Development of improved vaccines against whooping cough: current status. Hum. Vaccines 6, 543–553 (2010).
doi: 10.4161/hv.6.7.11413
Knight, J. B. et al. Immunogenicity and protective efficacy of a recombinant filamentous haemagglutinin from Bordetella pertussis. Clin. Exp. Immunol. 144, 543–551 (2006).
pubmed: 16734625
pmcid: 1941966
doi: 10.1111/j.1365-2249.2006.03097.x
Relman, D. A., Domenighini, M., Tuomanen, E., Rappuoli, R. & Falkow, S. Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence. Proc. Natl Acad. Sci. USA 86, 2637–2641 (1989).
pubmed: 2539596
pmcid: 286972
doi: 10.1073/pnas.86.8.2637
Weingart, C. L. & Weiss, A. A. Bordetella pertussis virulence factors affect phagocytosis by human neutrophils. Infect. Immun. 68, 1735–1739 (2000).
pubmed: 10679000
pmcid: 97341
doi: 10.1128/IAI.68.3.1735-1739.2000
Henderson, M. W. et al. Contribution of Bordetella filamentous hemagglutinin and adenylate cyclase toxin to suppression and evasion of interleukin-17-mediated inflammation. Infect. Immun. 80, 2061–2075 (2012).
pubmed: 22473603
pmcid: 3370597
doi: 10.1128/IAI.00148-12
McGuirk, P. & Mills, K. H. Direct anti-inflammatory effect of a bacterial virulence factor: IL-10-dependent suppression of IL-12 production by filamentous hemagglutinin from Bordetella pertussis. Eur. J. Immunol. 30, 415–422 (2000).
pubmed: 10671196
doi: 10.1002/1521-4141(200002)30:2<415::AID-IMMU415>3.0.CO;2-X
Trinchieri, G. Interleukin-12 and the regulation of innate resistance and adaptive immunity. Nat. Rev. Immunol. 3, 133–146 (2003).
pubmed: 12563297
doi: 10.1038/nri1001
Higgs, R., Higgins, S., Ross, P. & Mills, K. Immunity to the respiratory pathogen Bordetella pertussis. Mucosal. Immunol. 5, 485–500 (2012).
pubmed: 22718262
doi: 10.1038/mi.2012.54
Kimura, A., Mountzouros, K. T., Relman, D. A., Falkow, S. & Cowell, J. L. Bordetella pertussis filamentous hemagglutinin: evaluation as a protective antigen and colonization factor in a mouse respiratory infection model. Infect. Immun. 58, 7–16 (1990).
pubmed: 2294058
pmcid: 258400
doi: 10.1128/iai.58.1.7-16.1990
Mills, K. H., Ryan, M., Ryan, E. & Mahon, B. P. A murine model in which protection correlates with pertussis vaccine efficacy in children reveals complementary roles for humoral and cell-mediated immunity in protection against Bordetella pertussis. Infect. Immun. 66, 594–602 (1998).
pubmed: 9453614
pmcid: 107945
doi: 10.1128/IAI.66.2.594-602.1998
Goebel, E. M., Zhang, X. & Harvill, E. T. Bordetella pertussis infection or vaccination substantially protects mice against B. bronchiseptica infection. PLoS One 4, e6778 (2009).
pubmed: 19707559
pmcid: 2727957
doi: 10.1371/journal.pone.0006778
Goldberg, A., Fridman, O., Ronin, I. & Balaban, N. Q. Systematic identification and quantification of phase variation in commensal and pathogenic Escherichia coli. Genome Med. 6, 112 (2014).
pubmed: 25530806
pmcid: 4272514
doi: 10.1186/s13073-014-0112-4
Zeddeman, A. et al. Effect of FHA and Prn on Bordetella pertussis colonization of mice is dependent on vaccine type and anatomical site. Plos one 15, e0237394 (2020).
pubmed: 32822419
pmcid: 7446907
doi: 10.1371/journal.pone.0237394
Carbonetti, N. H. et al. Highlights of the 11th International Bordetella Symposium: from basic biology to vaccine development. Clin. Vaccin. Immunol. 23, 842–850 (2016).
doi: 10.1128/CVI.00388-16
Ciabattini, A. et al. Modulation of primary immune response by different vaccine adjuvants. Front. Immunol. 7, 427 (2016).
pubmed: 27781036
pmcid: 5066114
doi: 10.3389/fimmu.2016.00427
Howlader, D. R. et al. Development of a novel S. Typhi and Paratyphi A outer membrane vesicles based bivalent vaccine against enteric fever. PLoS One 13, e0203631 (2018).
pubmed: 30216367
pmcid: 6138408
doi: 10.1371/journal.pone.0203631
Yazdankhah, S. P. & Caugant, D. A. Neisseria meningitidis: an overview of the carriage state. J. Med. Microbiol. 53, 821–832 (2004).
pubmed: 15314188
doi: 10.1099/jmm.0.45529-0
Rosenstein, N. E. et al. The changing epidemiology of meningococcal disease in the United States, 1992–1996. J. Infect. Dis. 180, 1894–1901 (1999).
pubmed: 10558946
doi: 10.1086/315158
Tettelin, H. et al. Complete genome sequence of Neisseria meningitidis serogroup B strain MC58. Science 287, 1809–1815 (2000).
pubmed: 10710307
doi: 10.1126/science.287.5459.1809
Masignani, V., Pizza, M. & Moxon, E. R. The development of a vaccine against meningococcus B using reverse vaccinology. Front. Immunol. 10, 751 (2019).
pubmed: 31040844
pmcid: 6477034
doi: 10.3389/fimmu.2019.00751
Borrow, R. et al. Neisseria meningitidis group B correlates of protection and assay standardization-international meeting report Emory University, Atlanta, Georgia, United States, 16-17 March 2005. Vaccine 24, 5093–5107 (2006).
pubmed: 16838413
doi: 10.1016/j.vaccine.2006.03.091
Giuliani, M. M. et al. Measuring antigen-specific bactericidal responses to a multicomponent vaccine against serogroup B meningococcus. Vaccine 28, 5023–5030 (2010).
pubmed: 20493284
doi: 10.1016/j.vaccine.2010.05.014
Biolchi, A. et al. 4CMenB immunization induces serum bactericidal antibodies against non-serogroup B meningococcal strains in adolescents. Infect. Dis. Ther. 10, 307–316 (2021).
pubmed: 33185849
doi: 10.1007/s40121-020-00370-x
Biolchi, A. et al. Multicomponent meningococcal serogroup B vaccination elicits cross-reactive immunity in infants against genetically diverse serogroup C, W and Y invasive disease isolates. Vaccine 38, 7542–7550 (2020).
pubmed: 33036804
doi: 10.1016/j.vaccine.2020.09.050
Leduc, I. et al. The serogroup B meningococcal outer membrane vesicle-based vaccine 4CMenB induces cross-species protection against Neisseria gonorrhoeae. PLoS Pathog. 16, e1008602 (2020).
pubmed: 33290434
pmcid: 7748408
doi: 10.1371/journal.ppat.1008602
Reyes Díaz, L. M. et al. VA-MENGOC-BC vaccination induces serum and mucosal anti Neisseria gonorrhoeae immune responses and reduces the incidence of gonorrhea. Pediatr. Infect. Dis. J. 40, 375–381 (2021).
pubmed: 33591079
doi: 10.1097/INF.0000000000003047
Capecchi, B. et al. Neisseria meningitidis NadA is a new invasin which promotes bacterial adhesion to and penetration into human epithelial cells. Mol. Microbiol. 55, 687–698 (2005).
pubmed: 15660996
doi: 10.1111/j.1365-2958.2004.04423.x
Rodrigues, C. M. C. et al. Genomic surveillance of 4CMenB vaccine antigenic variants among disease-causing Neisseria meningitidis isolates, United Kingdom, 2010-2016. Emerg. Infect. Dis. 24, 673–682 (2018).
pubmed: 29553330
pmcid: 5875271
doi: 10.3201/eid2404.171480
Franzoso, S. et al. Human monocytes/macrophages are a target of Neisseria meningitidis Adhesin A (NadA). J. Leukoc. Biol. 83, 1100–1110 (2008).
pubmed: 18299457
doi: 10.1189/jlb.1207810
Giuliani, M. et al. Human protective response induced by meningococcus B vaccine is mediated by the synergy of multiple bactericidal epitopes. Sci. Rep. 8, 3700 (2018).
pubmed: 29487324
pmcid: 5829249
doi: 10.1038/s41598-018-22057-7
Tavano, R. et al. Mapping of the Neisseria meningitidis NadA cell-binding site: relevance of predicted {alpha}-helices in the NH2-terminal and dimeric coiled-coil regions. J. Bacteriol. 193, 107–115 (2011).
pubmed: 20971901
doi: 10.1128/JB.00430-10
Marr, N. et al. Protective activity of the Bordetella pertussis BrkA autotransporter in the murine lung colonization model. Vaccine 26, 4306–4311 (2008).
pubmed: 18582518
doi: 10.1016/j.vaccine.2008.06.017
de Gouw, D. et al. Proteomics-identified Bvg-activated autotransporters protect against Bordetella pertussis in a mouse model. PLoS One 9, e105011 (2014).
pubmed: 25133400
pmcid: 4136822
doi: 10.1371/journal.pone.0105011
Fusco, W. G. et al. The Haemophilus ducreyi trimeric autotransporter adhesin DsrA protects against an experimental infection in the swine model of chancroid. Vaccine 32, 3752–3758 (2014).
pubmed: 24844153
pmcid: 6267434
doi: 10.1016/j.vaccine.2014.05.031
Ysebaert, C. et al. UspA2 is a cross-protective Moraxella catarrhalis vaccine antigen. Vaccine 39, 5641–5649 (2021).
pubmed: 34446318
doi: 10.1016/j.vaccine.2021.08.002
Raghunathan, D. et al. SadA, a trimeric autotransporter from Salmonella enterica serovar Typhimurium, can promote biofilm formation and provides limited protection against infection. Infect. Immun. 79, 4342–4352 (2011).
pubmed: 21859856
pmcid: 3257908
doi: 10.1128/IAI.05592-11
Alamuri, P., Eaton, K. A., Himpsl, S. D., Smith, S. N. & Mobley, H. L. Vaccination with proteus toxic agglutinin, a hemolysin-independent cytotoxin in vivo, protects against Proteus mirabilis urinary tract infection. Infect. Immun. 77, 632–641 (2009).
pubmed: 19029299
doi: 10.1128/IAI.01050-08
León, Y. et al. Intranasal immunization of mice with multiepitope chimeric vaccine candidate based on conserved autotransporters SigA, Pic and Sap, confers protection against Shigella flexneri. Vaccines 8, 563 (2020).
pubmed: 33019492
pmcid: 7712744
doi: 10.3390/vaccines8040563
Winter, L. E. & Barenkamp, S. J. Immunogenicity of nontypeable Haemophilus influenzae outer membrane vesicles and protective ability in the chinchilla model of otitis media. Clin. Vaccine Immunol. 24, https://doi.org/10.1128/cvi.00138-17 (2017).
Okamura, M. et al. Immunization with outer membrane protein A from Salmonella enterica serovar Enteritidis induces humoral immune response but no protection against homologous challenge in chickens. Poult. Sci. 91, 2444–2449 (2012).
pubmed: 22991526
doi: 10.3382/ps.2012-02303
Jose, J. & Meyer, T. F. The autodisplay story, from discovery to biotechnical and biomedical applications. Microbiol Mol. Biol. Rev. 71, 600–619 (2007).
pubmed: 18063719
pmcid: 2168652
doi: 10.1128/MMBR.00011-07
Ruiz-Pérez, F. et al. Expression of the Plasmodium falciparum immunodominant epitope (NANP)(4) on the surface of Salmonella enterica using the autotransporter MisL. Infect. Immun. 70, 3611–3620 (2002).
pubmed: 12065502
pmcid: 128084
doi: 10.1128/IAI.70.7.3611-3620.2002
Lambert, L. C. Pertussis vaccine trials in the 1990s. J. Infect. Dis. 209, S4–S9 (2014).
pubmed: 24626871
pmcid: 3968808
doi: 10.1093/infdis/jit592
Clemens, J., Shin, S., Sur, D., Nair, G. B. & Holmgren, J. New-generation vaccines against cholera. Nat. Rev. Gastroenterol. Hepatol. 8, 701–710 (2011).
pubmed: 22064524
doi: 10.1038/nrgastro.2011.174
Meyer, K. F. Effectiveness of live or killed plague vaccines in man. Bull. World Health Organ 42, 653–666 (1970).
pubmed: 4988692
pmcid: 2427500
Fratzke, A. P., Gregory, A. E., van Schaik, E. J. & Samuel, J. E. Coxiella burnetii whole cell vaccine produces a Th1 delayed-type hypersensitivity response in a novel sensitized mouse model. Front. Immunol. 12, 754712 (2021).
pubmed: 34616410
pmcid: 8488435
doi: 10.3389/fimmu.2021.754712
Garmory, H. S., Brown, K. A. & Titball, R. W. Salmonella vaccines for use in humans: present and future perspectives. FEMS Microbiol. Rev. 26, 339–353 (2002).
pubmed: 12413664
Lange, C. et al. 100 years of Mycobacterium bovis bacille Calmette-Guérin. Lancet Infect. Dis. 22, e2–e12 (2022).
pubmed: 34506734
doi: 10.1016/S1473-3099(21)00403-5
Levine, M. M. et al. Duration of efficacy of Ty21a, attenuated Salmonella typhi live oral vaccine. Vaccine 17, S22–S27 (1999).
pubmed: 10506405
doi: 10.1016/S0264-410X(99)00231-5
Jia, Q. et al. A Francisella tularensis live vaccine strain (LVS) mutant with a deletion in capB, encoding a putative capsular biosynthesis protein, is significantly more attenuated than LVS yet induces potent protective immunity in mice against F. tularensis challenge. Infect. Immun. 78, 4341–4355 (2010).
pubmed: 20643859
pmcid: 2950357
doi: 10.1128/IAI.00192-10
Clark, A. & Wolfe, D. N. Current state of anthrax vaccines and key R&D gaps moving forward. Microorganisms 8, https://doi.org/10.3390/microorganisms8050651 (2020).
Mosley, J. F. et al. Vaxchora: the first FDA-approved cholera vaccination in the United States. P t 42, 638–640 (2017).
pubmed: 29018300
pmcid: 5614415
Beran, J., Dražan, D., Enweonye, I., Bhusal, C. & Toneatto, D. Immunogenicity and safety of investigational MenABCWY vaccine and of 4CMenB and MenACWY vaccines administered concomitantly or alone: a Phase 2 randomized study of adolescents and young adults. mSphere 6, e0055321 (2021).
pubmed: 34787449
doi: 10.1128/mSphere.00553-21
Vila-Corcoles, A. & Ochoa-Gondar, O. Preventing pneumococcal disease in the elderly: recent advances in vaccines and implications for clinical practice. Drugs Aging 30, 263–276 (2013).
pubmed: 23420119
doi: 10.1007/s40266-013-0060-5
Kelly, D. F., Moxon, E. R. & Pollard, A. J. Haemophilus influenzae type b conjugate vaccines. Immunology 113, 163–174 (2004).
pubmed: 15379976
pmcid: 1782565
doi: 10.1111/j.1365-2567.2004.01971.x
Cartee, R. T. et al. A phase 1 randomized safety, reactogenicity, and immunogenicity study of Typhax: A novel protein capsular matrix vaccine candidate for the prevention of typhoid fever. PLoS Negl. Trop. Dis. 14, e0007912 (2020).
pubmed: 31905228
pmcid: 6964911
doi: 10.1371/journal.pntd.0007912
Klein, N. P. Licensed pertussis vaccines in the United States. History and current state. Hum. Vaccin Immunother. 10, 2684–2690 (2014).
pubmed: 25483496
pmcid: 4975064
doi: 10.4161/hv.29576
Viviani, V., Biolchi, A. & Pizza, M. Synergistic activity of antibodies in the multicomponent 4CMenB vaccine. Expert Rev. Vaccines 21, 645–658 (2022).
pubmed: 35257644
doi: 10.1080/14760584.2022.2050697
Wood, N. et al. Immunogenicity and safety of monovalent acellular pertussis vaccine at birth: a randomized clinical trial. JAMA Pediatr. 172, 1045–1052 (2018).
pubmed: 30208475
pmcid: 6248137
doi: 10.1001/jamapediatrics.2018.2349
Comstedt, P., Schüler, W., Meinke, A. & Lundberg, U. The novel Lyme borreliosis vaccine VLA15 shows broad protection against Borrelia species expressing six different OspA serotypes. PLoS One 12, e0184357 (2017).
pubmed: 28863166
pmcid: 5581183
doi: 10.1371/journal.pone.0184357
Bentancor, L. V., Camacho-Peiro, A., Bozkurt-Guzel, C., Pier, G. B. & Maira-Litrán, T. Identification of Ata, a multifunctional trimeric autotransporter of Acinetobacter baumannii. J. Bacteriol. 194, 3950–3960 (2012).
pubmed: 22609912
pmcid: 3416510
doi: 10.1128/JB.06769-11
Bentancor, L. V. et al. Evaluation of the trimeric autotransporter Ata as a vaccine candidate against Acinetobacter baumannii infections. Infect. Immun. 80, 3381–3388 (2012).
pubmed: 22825448
pmcid: 3457567
doi: 10.1128/IAI.06096-11
Xiao, L. et al. Apa is a trimeric autotransporter adhesin of Actinobacillus pleuropneumoniae responsible for autoagglutination and host cell adherence. J. Basic Microbiol. 52, 598–607 (2012).
pubmed: 22143982
doi: 10.1002/jobm.201100365
Hathroubi, S., Loera-Muro, A., Guerrero-Barrera, A. L., Tremblay, Y. D. N. & Jacques, M. Actinobacillus pleuropneumoniae biofilms: role in pathogenicity and potential impact for vaccination development. Anim. Health Res. Rev. 19, 17–30 (2018).
pubmed: 29110751
doi: 10.1017/S146625231700010X
Siewert, L. K. et al. Identification of the Bartonella autotransporter CFA as a protective antigen and hypervariable target of neutralizing antibodies in mice. Proc. Natl Acad. Sci. USA 119, e2202059119 (2022).
pubmed: 35714289
pmcid: 9231624
doi: 10.1073/pnas.2202059119
Ruiz-Ranwez, V. et al. The BtaF trimeric autotransporter of Brucella suis is involved in attachment to various surfaces, resistance to serum and virulence. PLoS One 8, e79770 (2013).
pubmed: 24236157
pmcid: 3827427
doi: 10.1371/journal.pone.0079770
Muñoz González, F. et al. The BtaF adhesin is necessary for full virulence during respiratory infection by Brucella suis and is a novel immunogen for nasal vaccination against Brucella infection. Front. Immunol. 10, 1775 (2019).
pubmed: 31402921
pmcid: 6676368
doi: 10.3389/fimmu.2019.01775
Kiessling, A. R., Malik, A. & Goldman, A. Recent advances in the understanding of trimeric autotransporter adhesins. Med. Microbiol. Immunol. 209, 233–242 (2020).
pubmed: 31865405
doi: 10.1007/s00430-019-00652-3
Lafontaine, E. R. et al. The autotransporter protein BatA is a protective antigen against lethal aerosol infection with Burkholderia mallei and Burkholderia pseudomallei. Vaccin. X 1, 100002 (2019).
doi: 10.1016/j.jvacx.2018.100002
Crane, D. D. et al. Chlamydia trachomatis polymorphic membrane protein D is a species-common pan-neutralizing antigen. Proc. Natl Acad. Sci. USA 103, 1894–1899 (2006).
pubmed: 16446444
pmcid: 1413641
doi: 10.1073/pnas.0508983103
Swanson, K. A. et al. Chlamydia trachomatis polymorphic membrane protein D is an oligomeric autotransporter with a higher-order structure. Infect. Immun. 77, 508–516 (2009).
pubmed: 19001072
doi: 10.1128/IAI.01173-08
Hu, Y. H., Zhou, H. Z., Jin, Q. W. & Zhang, J. The serine protease autotransporter Tsh contributes to the virulence of Edwardsiella tarda. Vet. Microbiol 189, 68–74 (2016).
pubmed: 27259829
doi: 10.1016/j.vetmic.2016.04.021
Ulett, G. C. et al. Functional analysis of antigen 43 in uropathogenic Escherichia coli reveals a role in long-term persistence in the urinary tract. Infect. Immun. 75, 3233–3244 (2007).
pubmed: 17420234
pmcid: 1932929
doi: 10.1128/IAI.01952-06
Harris, J. A. et al. Directed evaluation of enterotoxigenic Escherichia coli autotransporter proteins as putative vaccine candidates. PLoS Negl. Trop. Dis. 5, e1428–e1428 (2011).
pubmed: 22163060
pmcid: 3232201
doi: 10.1371/journal.pntd.0001428
Chakraborty, S. et al. Human experimental challenge with enterotoxigenic Escherichia coli elicits immune responses to canonical and novel antigens relevant to vaccine development. J. Infect. Dis. 218, 1436–1446 (2018).
pubmed: 29800314
pmcid: 6151082
doi: 10.1093/infdis/jiy312
Xing, Y. et al. Broad protective vaccination against systemic Escherichia coli with autotransporter antigens. PLoS Pathog. 19, e1011082 (2023).
pubmed: 36800400
pmcid: 9937491
doi: 10.1371/journal.ppat.1011082
Hendrixson, D. R. & Geme, J. W. S.III. The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein. Mol. cell 2, 841–850 (1998).
Cutter, D. et al. Immunization with Haemophilus influenzae Hap adhesin protects against nasopharyngeal colonization in experimental mice. J. Infect. Dis. 186, 1115–1121 (2002).
pubmed: 12355362
doi: 10.1086/344233
Olvera, A. et al. Immunogenicity and protection against Haemophilus parasuis infection after vaccination with recombinant virulence associated trimeric autotransporters (VtaA). Vaccine 29, 2797–2802 (2011).
pubmed: 21320547
doi: 10.1016/j.vaccine.2011.01.105
Echenique-Rivera, H. et al. A naturally occurring single-residue mutation in the translocator domain of Neisseria meningitidis NhhA affects trimerization, surface localization, and adhesive capabilities. Infect. Immun. 79, 4308–4321 (2011).
pubmed: 21844231
pmcid: 3257927
doi: 10.1128/IAI.00198-11
Ha, N. Y. et al. Immunization with an autotransporter protein of Orientia tsutsugamushi provides protective immunity against scrub typhus. PLoS Negl. Trop. Dis. 9, e0003585 (2015).
pubmed: 25768004
pmcid: 4359152
doi: 10.1371/journal.pntd.0003585
Bianconi, I. et al. Genome-based approach delivers vaccine candidates against Pseudomonas aeruginosa. Front. Immunol. 9, https://doi.org/10.3389/fimmu.2018.03021 (2019).
Dorsey, C. W., Laarakker, M. C., Humphries, A. D., Weening, E. H. & Bäumler, A. J. Salmonella enterica serotype Typhimurium MisL is an intestinal colonization factor that binds fibronectin. Mol. Microbiol. 57, 196–211 (2005).
pubmed: 15948960
doi: 10.1111/j.1365-2958.2005.04666.x
Paton, A. W., Srimanote, P., Woodrow, M. C. & Paton, J. C. Characterization of Saa, a novel autoagglutinating adhesin produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains that are virulent for humans. Infect. Immun. 69, 6999–7009 (2001).
pubmed: 11598075
pmcid: 100080
doi: 10.1128/IAI.69.11.6999-7009.2001
Coster, T. S. et al. Vaccination against shigellosis with attenuated Shigella flexneri 2a strain SC602. Infect. Immun. 67, 3437–3443 (1999).
pubmed: 10377124
pmcid: 116529
doi: 10.1128/IAI.67.7.3437-3443.1999
Mantis, N. J., Rol, N. & Corthésy, B. Secretory IgA’s complex roles in immunity and mucosal homeostasis in the gut. Mucosal. Immunol. 4, 603–611 (2011).
pubmed: 21975936
pmcid: 3774538
doi: 10.1038/mi.2011.41
Tsugo, K., Nakamura, S. I., Yamanaka, H. & Une, Y. A study on the efficacy of the recombinant Yersinia adhesin A vaccine against yersiniosis in the early phase. J. Vet. Med. Sci. 79, 855–863 (2017).
pubmed: 28320976
pmcid: 5447973
doi: 10.1292/jvms.16-0528
Mirdita, M. et al. ColabFold: making protein folding accessible to all. Nat. Methods 19, 679–682 (2022).
pubmed: 35637307
pmcid: 9184281
doi: 10.1038/s41592-022-01488-1
Hanson, S. E., Dowdy, T., Larion, M., Doyle, M. T. & Bernstein, H. D. The patatin-like protein PlpD forms structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane. Nat. Commun. 15, 4389 (2024).
pubmed: 38782915
pmcid: 11116518
doi: 10.1038/s41467-024-48756-6