Altered TMPRSS2 usage by SARS-CoV-2 Omicron impacts infectivity and fusogenicity.

Adult Aged Aged, 80 and over Angiotensin-Converting Enzyme 2 / metabolism Animals Antibodies, Neutralizing / immunology Antibodies, Viral / immunology COVID-19 / immunology COVID-19 Vaccines / immunology Cell Line Cell Membrane / metabolism Chlorocebus aethiops Convalescence Female Humans Immune Sera / immunology Intestines / pathology Lung / pathology Male Membrane Fusion Middle Aged Mutation Nasal Mucosa / pathology SARS-CoV-2 / drug effects Serine Endopeptidases / metabolism Spike Glycoprotein, Coronavirus / genetics Tissue Culture Techniques Virulence Virus Internalization Virus Replication

Journal

Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462

Informations de publication

Date de publication:
03 2022
Historique:
received: 21 12 2021
accepted: 26 01 2022
pubmed: 2 2 2022
medline: 1 4 2022
entrez: 1 2 2022
Statut: ppublish

Résumé

The SARS-CoV-2 Omicron BA.1 variant emerged in 2021

Identifiants

DOI: 10.1038/s41586-022-04474-x PMID: 35104837 PMC: PMC8942856
pubmed: 35104837
doi: 10.1038/s41586-022-04474-x
pii: 10.1038/s41586-022-04474-x
pmc: PMC8942856
doi:

Substances chimiques

Antibodies, Neutralizing 0
Antibodies, Viral 0
COVID-19 Vaccines 0
Immune Sera 0
Spike Glycoprotein, Coronavirus 0
spike protein, SARS-CoV-2 0
ACE2 protein, human EC 3.4.17.23
Angiotensin-Converting Enzyme 2 EC 3.4.17.23
Serine Endopeptidases EC 3.4.21.-
TMPRSS2 protein, human EC 3.4.21.-

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

706-714

Subventions

Organisme : Medical Research Council
ID : MC_PC_17230
Pays : United Kingdom
Organisme : NIAID NIH HHS
ID : DP1 AI158186
Pays : United States
Organisme : Wellcome Trust
ID : 200594/Z/16/Z
Pays : United Kingdom
Organisme : Howard Hughes Medical Institute
Pays : United States
Organisme : Medical Research Council
ID : MC_UP_1201/16
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/P008801/1
Pays : United Kingdom
Organisme : NIAID NIH HHS
ID : HHSN272201700059C
Pays : United States
Organisme : Wellcome Trust
ID : WT108082AIA
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : T32 GM008268
Pays : United States
Organisme : Medical Research Council
ID : MC_U105181010
Pays : United Kingdom
Organisme : NIAID NIH HHS
ID : R01 AI138546
Pays : United States

Investigateurs

Stephen Baker (S)
Gordon Dougan (G)
Christoph Hess (C)
Nathalie Kingston (N)
Paul J Lehner (PJ)
Paul A Lyons (PA)
Nicholas J Matheson (NJ)
Willem H Ouwehand (WH)
Caroline Saunders (C)
Charlotte Summers (C)
James E D Thaventhiran (JED)
Mark Toshner (M)
Michael P Weekes (MP)
Patrick Maxwell (P)
Ashley Shaw (A)
Ashlea Bucke (A)
Jo Calder (J)
Laura Canna (L)
Jason Domingo (J)
Anne Elmer (A)
Stewart Fuller (S)
Julie Harris (J)
Sarah Hewitt (S)
Jane Kennet (J)
Sherly Jose (S)
Jenny Kourampa (J)
Anne Meadows (A)
Criona O'Brien (C)
Jane Price (J)
Cherry Publico (C)
Rebecca Rastall (R)
Carla Ribeiro (C)
Jane Rowlands (J)
Valentina Ruffolo (V)
Hugo Tordesillas (H)
Ben Bullman (B)
Benjamin J Dunmore (BJ)
Stefan Gräf (S)
Josh Hodgson (J)
Christopher Huang (C)
Kelvin Hunter (K)
Emma Jones (E)
Ekaterina Legchenko (E)
Cecilia Matara (C)
Jennifer Martin (J)
Federica Mescia (F)
Ciara O'Donnell (C)
Linda Pointon (L)
Joy Shih (J)
Rachel Sutcliffe (R)
Tobias Tilly (T)
Carmen Treacy (C)
Zhen Tong (Z)
Jennifer Wood (J)
Marta Wylot (M)
Ariana Betancourt (A)
Georgie Bower (G)
Chiara Cossetti (C)
Aloka De Sa (A)
Madeline Epping (M)
Stuart Fawke (S)
Nick Gleadall (N)
Richard Grenfell (R)
Andrew Hinch (A)
Sarah Jackson (S)
Isobel Jarvis (I)
Ben Krishna (B)
Francesca Nice (F)
Ommar Omarjee (O)
Marianne Perera (M)
Martin Potts (M)
Nathan Richoz (N)
Veronika Romashova (V)
Luca Stefanucci (L)
Mateusz Strezlecki (M)
Lori Turner (L)
Eckart M D D De Bie (EMDD)
Katherine Bunclark (K)
Masa Josipovic (M)
Michael Mackay (M)
Helen Butcher (H)
Daniela Caputo (D)
Matt Chandler (M)
Patrick Chinnery (P)
Debbie Clapham-Riley (D)
Eleanor Dewhurst (E)
Christian Fernandez (C)
Anita Furlong (A)
Barbara Graves (B)
Jennifer Gray (J)
Sabine Hein (S)
Tasmin Ivers (T)
Emma Le Gresley (E)
Rachel Linger (R)
Mary Kasanicki (M)
Rebecca King (R)
Nathalie Kingston (N)
Sarah Meloy (S)
Alexei Moulton (A)
Francesca Muldoon (F)
Nigel Ovington (N)
Sofia Papadia (S)
Christopher J Penkett (CJ)
Isabel Phelan (I)
Venkatesh Ranganath (V)
Roxana Paraschiv (R)
Abigail Sage (A)
Jennifer Sambrook (J)
Ingrid Scholtes (I)
Katherine Schon (K)
Hannah Stark (H)
Kathleen E Stirrups (KE)
Paul Townsend (P)
Neil Walker (N)
Jennifer Webster (J)
Erika P Butlertanaka (EP)
Yuri L Tanaka (YL)
Jumpei Ito (J)
Keiya Uriu (K)
Yusuke Kosugi (Y)
Mai Suganami (M)
Akiko Oide (A)
Miyabishara Yokoyama (M)
Mika Chiba (M)
Chihiro Motozono (C)
Hesham Nasser (H)
Ryo Shimizu (R)
Kazuko Kitazato (K)
Haruyo Hasebe (H)
Takashi Irie (T)
So Nakagawa (S)
Jiaqi Wu (J)
Miyoko Takahashi (M)
Takasuke Fukuhara (T)
Kenta Shimizu (K)
Kana Tsushima (K)
Haruko Kubo (H)
Yasuhiro Kazuma (Y)
Ryosuke Nomura (R)
Yoshihito Horisawa (Y)
Kayoko Nagata (K)
Yugo Kawai (Y)
Yohei Yanagida (Y)
Yusuke Tashiro (Y)
Kenzo Tokunaga (K)
Seiya Ozono (S)
Ryoko Kawabata (R)
Nanami Morizako (N)
Kenji Sadamasu (K)
Hiroyuki Asakura (H)
Mami Nagashima (M)
Kazuhisa Yoshimura (K)
Paúl Cárdenas (P)
Erika Muñoz (E)
Veronica Barragan (V)
Sully Márquez (S)
Belén Prado-Vivar (B)
Mónica Becerra-Wong (M)
Mateo Caravajal (M)
Gabriel Trueba (G)
Patricio Rojas-Silva (P)
Michelle Grunauer (M)
Bernardo Gutierrez (B)
Juan José Guadalupe (JJ)
Juan Carlos Fernández-Cadena (JC)
Derly Andrade-Molina (D)
Manuel Baldeon (M)
Andrea Pinos (A)

Commentaires et corrections

Type : UpdateOf
Type : CommentIn

Informations de copyright

© 2022. The Author(s).

Références

Viana, R. et al. Rapid epidemic expansion of the SARS-CoV-2 Omicron variant in southern Africa. Nature https://doi.org/10.1038/s41586-022-04411-y (2022).
Cele, S. et al. Omicron extensively but incompletely escapes Pfizer BNT162b2 neutralization. Nature https://doi.org/10.1038/s41586-021-04387-1 (2021).
Hoffmann, M. et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell 181, 271–280 (2020).
pubmed: 32142651 pmcid: 7102627
Mlcochova, P. et al. SARS-CoV-2 B.1.617.2 Delta variant replication and immune evasion. Nature 599, 114–119 (2021).
pubmed: 34488225 pmcid: 8566220 doi: 10.1038/s41586-021-03944-y
Meng, B. et al. Recurrent emergence of SARS-CoV-2 spike deletion H69/V70 and its role in the Alpha variant B.1.1.7. Cell Rep. 35, 109292 (2021).
pubmed: 34166617 pmcid: 8185188 doi: 10.1016/j.celrep.2021.109292
Saito, A. et al. Enhanced fusogenicity and pathogenicity of SARS-CoV-2 Delta P681R mutation. Nature 602, 300–306 (2021).
pubmed: 34823256 pmcid: 8828475
Peacock, T. P. et al. The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets. Nat. Microbiol. 6, 899–909 (2021).
pubmed: 33907312 doi: 10.1038/s41564-021-00908-w
Dejnirattisai, W. et al. Reduced neutralisation of SARS-COV-2 Omicron-B.1.1.529 variant by post-immunisation serum. Lancet 399, 234–236 (2021).
pubmed: 34942101 pmcid: 8687667 doi: 10.1016/S0140-6736(21)02844-0
Wolter, N. et al. Early assessment of the clinical severity of the SARS-CoV-2 Omicron variant in South Africa: a data linkage study. Lancet https://doi.org/10.1016/S0140-6736(22)00017-4 (2022).
Walls, A. C. et al. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 181, 281–292 (2020).
pubmed: 32155444 pmcid: 7102599 doi: 10.1016/j.cell.2020.02.058
Cameroni, E. et al. Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift. Nature https://doi.org/10.1038/s41586-021-04386-2 (2021).
Starr, T. N. et al. Deep mutational scanning of SARS-CoV-2 receptor binding domain reveals constraints on folding and ACE2 binding. Cell 182, 1295–1310 (2020).
pubmed: 32841599 pmcid: 7418704 doi: 10.1016/j.cell.2020.08.012
McCallum, M. et al. Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants. Science 374, 1621–1626 (2021).
pubmed: 34751595 doi: 10.1126/science.abl8506
Collier, D. A. et al. SARS-CoV-2 B.1.1.7 sensitivity to mRNA vaccine-elicited, convalescent and monoclonal antibodies. Nature 593, 136–141 (2021).
pubmed: 33706364 doi: 10.1038/s41586-021-03412-7
McCallum, M. et al. Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement. Science https://doi.org/10.1126/science.abn8652 (2021).
Barnes, C. O. et al. SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies. Nature 588, 682–687 (2020).
pubmed: 33045718 pmcid: 8092461 doi: 10.1038/s41586-020-2852-1
Naldini, L. et al. In vivo gene delivery and stable transduction of non-dividing cells by a lentiviral vector. Science 272, 263–267 (1996).
pubmed: 8602510 doi: 10.1126/science.272.5259.263
Mlcochova, P. et al. Combined point of care nucleic acid and antibody testing for SARS-CoV-2 following emergence of D614G spike variant. Cell Rep. Med. 1, 100099 (2020).
pubmed: 32905045 pmcid: 7462534 doi: 10.1016/j.xcrm.2020.100099
Pommerenke, C. et al. Identification of cell lines CL-14, CL-40 and CAL-51 as suitable models for SARS-CoV-2 infection studies. PLoS ONE 16, e0255622 (2021).
pubmed: 34339474 pmcid: 8328321 doi: 10.1371/journal.pone.0255622
Youk, J. et al. Three-dimensional human alveolar stem cell culture models reveal infection response to SARS-CoV-2. Cell Stem Cell 27, 905–919 (2020).
pubmed: 33142113 pmcid: 7577700 doi: 10.1016/j.stem.2020.10.004
Sachs, N. et al. Long-term expanding human airway organoids for disease modeling. EMBO J. 38, e100300 (2019).
pubmed: 30643021 pmcid: 6376275 doi: 10.15252/embj.2018100300
Papa, G. et al. Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusion. PLoS Pathog. 17, e1009246 (2021).
pubmed: 33493182 pmcid: 7861537 doi: 10.1371/journal.ppat.1009246
Ou, T. et al. Hydroxychloroquine-mediated inhibition of SARS-CoV-2 entry is attenuated by TMPRSS2. PLoS Pathog. 17, e1009212 (2021).
pubmed: 33465165 pmcid: 7845965 doi: 10.1371/journal.ppat.1009212
Madissoon, E. et al. A spatial multi-omics atlas of the human lung reveals a novel immune cell survival niche. Preprint at https://doi.org/10.1101/2021.11.26.470108 (2021).
Salahudeen, A. A. et al. Progenitor identification and SARS-CoV-2 infection in human distal lung organoids. Nature 588, 670–675 (2020).
pubmed: 33238290 pmcid: 8003326 doi: 10.1038/s41586-020-3014-1
Brevini, T. et al. FXR inhibition reduces ACE2 expression, SARS-CoV-2 infection and may improve COVID-19 outcome. Preprint at https://doi.org/10.1101/2021.06.06.446781 (2021).
Buchrieser, J. et al. Syncytia formation by SARS-CoV-2-infected cells. EMBO J. 40, e107405 (2021).
pubmed: 33522642 pmcid: 7849166 doi: 10.15252/embj.2020107405
Cattin-Ortolá, J. et al. Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facilitate expression at the cell surface and syncytia formation. Nat. Commun. 12, 5333 (2021).
Li, W. et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426, 450–454 (2003).
pubmed: 14647384 pmcid: 7095016 doi: 10.1038/nature02145
Braga, L. et al. Drugs that inhibit TMEM16 proteins block SARS-CoV-2 Spike-induced syncytia. Nature 594, 88–93 (2021).
pubmed: 33827113 pmcid: 7611055 doi: 10.1038/s41586-021-03491-6
Bussani, R. et al. Persistence of viral RNA, pneumocyte syncytia and thrombosis are hallmarks of advanced COVID-19 pathology. eBioMedicine 61, 103104 (2020).
pubmed: 33158808 pmcid: 7677597 doi: 10.1016/j.ebiom.2020.103104
Ferreira, I. et al. SARS-CoV-2 B.1.617 mutations L452R and E484Q are not synergistic for antibody evasion. J. Infect. Dis. 224, 989–994 (2021).
pubmed: 34260717 pmcid: 8420622 doi: 10.1093/infdis/jiab368
Meng, B. et al. Recurrent emergence and transmission of a SARS-CoV-2 spike deletion H69/V70 and role in Alpha variant B.1.1.7. Cell Rep. 35, 109292 (2021).
pubmed: 34166617 pmcid: 8185188 doi: 10.1016/j.celrep.2021.109292
Cabantous, S., Terwilliger, T. C. & Waldo, G. S. Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat. Biotechnol. 23, 102–107 (2005).
pubmed: 15580262 doi: 10.1038/nbt1044
Cathcart, A. L. et al. The dual function monoclonal antibodies VIR-7831 and VIR-7832 demonstrate potent in vitro and in vivo activity against SARS-CoV-2. Preprint at https://doi.org/10.1101/2021.03.09.434607 (2021).
V’Kovski, P., Kratzel, A., Steiner, S., Stalder, H. & Thiel, V. Coronavirus biology and replication: implications for SARS-CoV-2. Nat. Rev. Microbiol. 19, 155–170 (2021).
pubmed: 33116300 doi: 10.1038/s41579-020-00468-6
Bugge, T. H., Antalis, T. M. & Wu, Q. Type II transmembrane serine proteases. J. Biol. Chem. 284, 23177–23181 (2009).
pubmed: 19487698 pmcid: 2749090 doi: 10.1074/jbc.R109.021006
Park, J. E. et al. Proteolytic processing of Middle East respiratory syndrome coronavirus spikes expands virus tropism. Proc. Natl Acad. Sci. USA 113, 12262–12267 (2016).
pubmed: 27791014 pmcid: 5086990 doi: 10.1073/pnas.1608147113
Shuai, H. et al. Attenuated replication and pathogenesis of SARS-CoV-2 B.1.1.529 Omicron. Nature https://doi.org/10.1038/s41586-022-04442-5 (2021).
Heurich, A. et al. TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein. J. Virol. 88, 1293–1307 (2014).
pubmed: 24227843 pmcid: 3911672 doi: 10.1128/JVI.02202-13
Katoh, K. & Standley, D. M. MAFFT multiple sequence alignment software version 7: improvements in performance and usability. Mol. Biol. Evol. 30, 772–780 (2013).
pubmed: 23329690 pmcid: 3603318 doi: 10.1093/molbev/mst010
Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583–589 (2021).
pubmed: 34265844 pmcid: 8371605 doi: 10.1038/s41586-021-03819-2
Goddard, T. D. et al. UCSF ChimeraX: meeting modern challenges in visualization and analysis. Protein Sci. 27, 14–25 (2018).
pubmed: 28710774
Motozono, C. et al. SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity. Cell Host Microbe 29, 1124–1136 (2021).
pubmed: 34171266 pmcid: 8205251 doi: 10.1016/j.chom.2021.06.006
Matsuyama, S. et al. Enhanced isolation of SARS-CoV-2 by TMPRSS2-expressing cells. Proc. Natl Acad. Sci. USA 117, 7001–7003 (2020).
pubmed: 32165541 pmcid: 7132130 doi: 10.1073/pnas.2002589117
Dejnirattisai, W. et al. SARS-CoV2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses. Cell 185, 467–484.e15 (2022).
Dejnirattisai, W. et al. Reduced neutralisation of SARS-CoV-2 omicron B.1.1.529 variant by post-immunisation serum. Lancet 399, 234–236 (2022).
pubmed: 34942101 doi: 10.1016/S0140-6736(21)02844-0
Itokawa, K., Sekizuka, T., Hashino, M., Tanaka, R. & Kuroda, M. Disentangling primer interactions improves SARS-CoV-2 genome sequencing by multiplex tiling PCR. PLoS ONE 15, e0239403 (2020).
pubmed: 32946527 pmcid: 7500614 doi: 10.1371/journal.pone.0239403
Bolger, A. M., Lohse, M. & Usadel, B. Trimmomatic: a flexible trimmer for Illumina sequence data. Bioinformatics 30, 2114–2120 (2014).
pubmed: 24695404 pmcid: 4103590 doi: 10.1093/bioinformatics/btu170
Langmead, B. & Salzberg, S. L. Fast gapped-read alignment with Bowtie 2. Nat. Methods 9, 357–359 (2012).
pubmed: 22388286 pmcid: 3322381
Chen, S. et al. Gencore: an efficient tool to generate consensus reads for error suppressing and duplicate removing of NGS data. BMC Bioinform. 20, 606 (2019).
doi: 10.1186/s12859-019-3280-9
Thorvaldsdottir, H., Robinson, J. T. & Mesirov, J. P. Integrative Genomics Viewer (IGV): high-performance genomics data visualization and exploration. Brief. Bioinform. 14, 178–192 (2013).
pubmed: 22517427 doi: 10.1093/bib/bbs017
Kimura, I. et al. The SARS-CoV-2 Lambda variant exhibits enhanced infectivity and immune resistance. Cell Rep 38, 110218 (2021).
pubmed: 34968415 pmcid: 8683271 doi: 10.1016/j.celrep.2021.110218
Vermeire, J. et al. Quantification of reverse transcriptase activity by real-time PCR as a fast and accurate method for titration of HIV, lenti- and retroviral vectors. PLoS ONE 7, e50859 (2012).
pubmed: 23227216 pmcid: 3515444 doi: 10.1371/journal.pone.0050859
Gerber, P. P. et al. A protease-activatable luminescent biosensor and reporter cell line for authentic SARS-CoV-2 infection. PLoS Pathog. https://doi.org/10.1371/journal.ppat.1010265 (2022).
French, A. P., Mills, S., Swarup, R., Bennett, M. J. & Pridmore, T. P. Colocalization of fluorescent markers in confocal microscope images of plant cells. Nat. Protoc. 3, 619–628 (2008).
pubmed: 18388944 doi: 10.1038/nprot.2008.31

Auteurs

Bo Meng (B)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.

Adam Abdullahi (A)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.

Isabella A T M Ferreira (IATM)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.

Niluka Goonawardane (N)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.

Akatsuki Saito (A)

Department of Veterinary Science, Faculty of Agriculture, University of Miyazaki, Miyazaki, Japan.

Izumi Kimura (I)

Division of Systems Virology, Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.

Daichi Yamasoba (D)

Division of Systems Virology, Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.

Pehuén Pereyra Gerber (PP)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.

Saman Fatihi (S)

CSIR Institute of Genomics and Integrative Biology, Delhi, India.

Surabhi Rathore (S)

CSIR Institute of Genomics and Integrative Biology, Delhi, India.

Samantha K Zepeda (SK)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

Guido Papa (G)

MRC-Laboratory of Molecular Biology, Cambridge, UK.

Steven A Kemp (SA)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.

Terumasa Ikeda (T)

Division of Molecular Virology and Genetics, Joint Research Center for Human Retrovirus Infection, Kumamoto University, Kumamoto, Japan.

Mako Toyoda (M)

Division of Infection and Immunity, Joint Research Center for Human Retrovirus Infection, Kumamoto University, Kumamoto, Japan.

Toong Seng Tan (TS)

Division of Infection and Immunity, Joint Research Center for Human Retrovirus Infection, Kumamoto University, Kumamoto, Japan.

Jin Kuramochi (J)

Kuramochi Clinic Interpark, Utsunomiya, Japan.

Shigeki Mitsunaga (S)

Human Genetics Laboratory, National Institute of Genetics, Mishima, Japan.

Takamasa Ueno (T)

Division of Infection and Immunity, Joint Research Center for Human Retrovirus Infection, Kumamoto University, Kumamoto, Japan.

Kotaro Shirakawa (K)

Department of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.

Akifumi Takaori-Kondo (A)

Department of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.

Teresa Brevini (T)

Department of Medicine, University of Cambridge, Cambridge, UK.

Donna L Mallery (DL)

MRC-Laboratory of Molecular Biology, Cambridge, UK.

Oscar J Charles (OJ)

Division of Infection and Immunity, UCL, London, UK.

John E Bowen (JE)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

Anshu Joshi (A)

Department of Biochemistry, University of Washington, Seattle, WA, USA.

Alexandra C Walls (AC)

Department of Biochemistry, University of Washington, Seattle, WA, USA.
Department of Virology, University of Cambridge, Cambridge, UK.

Laurelle Jackson (L)

Africa Health Research Institute, Durban, South Africa.

Darren Martin (D)

University of Cape Town, Cape Town, South Africa.

Kenneth G C Smith (KGC)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.

John Bradley (J)

Department of Medicine, University of Cambridge, Cambridge, UK.

John A G Briggs (JAG)

Max Planck Institute of Biochemistry, Martinsried, Germany.

Jinwook Choi (J)

Wellcome-MRC Cambridge Stem Cell Institute, Cambridge, UK.

Elo Madissoon (E)

Welcome Sanger Institute, Wellcome Trust Genome Campus, Hinxton, UK.
European Molecular Biology Laboratory, European Bioinformatics Institute, EMBL-EBI, Wellcome Trust Genome Campus, Hinxton, UK.

Kerstin B Meyer (KB)

Welcome Sanger Institute, Wellcome Trust Genome Campus, Hinxton, UK.

Petra Mlcochova (P)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.

Lourdes Ceron-Gutierrez (L)

Addenbrooke's Hospital, Cambridge University Hospitals NHS Foundation Trust, Cambridge Biomedical Campus, Cambridge, UK.

Rainer Doffinger (R)

Addenbrooke's Hospital, Cambridge University Hospitals NHS Foundation Trust, Cambridge Biomedical Campus, Cambridge, UK.

Sarah A Teichmann (SA)

Welcome Sanger Institute, Wellcome Trust Genome Campus, Hinxton, UK.
Cavendish Laboratory, Department of Physics, University of Cambridge, Cambridge, UK.

Andrew J Fisher (AJ)

Transplant and Regenerative Medicine Laboratory, Translational and Clinical Research Institute, Faculty of Medical Sciences, Newcastle University, Newcastle Upon Tyne, UK.

Matteo S Pizzuto (MS)

Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland.

Anna de Marco (A)

Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland.

Davide Corti (D)

Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland.

Myra Hosmillo (M)

Department of Virology, University of Cambridge, Cambridge, UK.

Joo Hyeon Lee (JH)

Wellcome-MRC Cambridge Stem Cell Institute, Cambridge, UK.
Department of Physiology, Development and Neuroscience, University of Cambridge, Cambridge, UK.

Leo C James (LC)

MRC-Laboratory of Molecular Biology, Cambridge, UK.

Lipi Thukral (L)

CSIR Institute of Genomics and Integrative Biology, Delhi, India.

David Veesler (D)

Department of Biochemistry, University of Washington, Seattle, WA, USA.
Howard Hughes Medical Institute, Seattle, WA, USA.

Alex Sigal (A)

Africa Health Research Institute, Durban, South Africa.
Max Planck Institute for Infection Biology, Berlin, Germany.
School of Laboratory Medicine and Medical Sciences, University of KwaZulu-Natal, Durban, South Africa.

Fotios Sampaziotis (F)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.
Wellcome-MRC Cambridge Stem Cell Institute, Cambridge, UK.
Addenbrooke's Hospital, Cambridge University Hospitals NHS Foundation Trust, Cambridge Biomedical Campus, Cambridge, UK.

Ian G Goodfellow (IG)

Department of Virology, University of Cambridge, Cambridge, UK.

Nicholas J Matheson (NJ)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK.
Department of Medicine, University of Cambridge, Cambridge, UK.
Addenbrooke's Hospital, Cambridge University Hospitals NHS Foundation Trust, Cambridge Biomedical Campus, Cambridge, UK.
NHS Blood and Transplant, Cambridge, UK.

Kei Sato (K)

Division of Systems Virology, Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan. keisato@g.ecc.u-tokyo.ac.jp.
CREST, Japan Science and Technology Agency, Saitama, Japan. keisato@g.ecc.u-tokyo.ac.jp.

Ravindra K Gupta (RK)

Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Cambridge, UK. rkg20@cam.ac.uk.
Department of Medicine, University of Cambridge, Cambridge, UK. rkg20@cam.ac.uk.
Africa Health Research Institute, Durban, South Africa. rkg20@cam.ac.uk.
ORCID: 0000-0001-9751-1808

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female

Evaluation of Low-Value Services Across Major Medicare Advantage Insurers and Traditional Medicare.

Ciara Duggan, Adam L Beckman, Ishani Ganguli et al.
1.00
Humans United States Aged Cross-Sectional Studies Medicare Part C

Effectiveness of Virtual Yoga for Chronic Low Back Pain: A Randomized Clinical Trial.

Hallie Tankha, Devyn Gaskins, Amanda Shallcross et al.
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH

questionsmedicales.fr › Personnes › Tranches d'âge › Adulte › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Personnes › Tranches d'âge › Adulte › Sujet âgé › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Personnes › Tranches d'âge › Adulte › Sujet âgé › Sujet âgé de 80 ans ou plus › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Peptide hydrolases › Exopeptidases › Carboxypeptidases › Angiotensin-converting enzyme 2 › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Eucaryotes › Animaux › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Globulines › Sérum-globulines › Immunoglobulines › Anticorps › Anticorps neutralisants › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Globulines › Sérum-globulines › Immunoglobulines › Anticorps › Anticorps antiviraux › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Maladies de l'appareil respiratoire › Infections de l'appareil respiratoire › Pneumopathie infectieuse › Pneumopathie virale › COVID-19 › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Mélanges complexes › Produits biologiques › Vaccins › Vaccins antiviraux › Vaccins contre la COVID-19 › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Cellules › Cellules cultivées › Lignée cellulaire › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Cellules › Structures cellulaires › Membrane cellulaire › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Cercopithecidae › Cercopithecinae › Cercopithecus › Cercopithecus aethiops › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › États, signes et symptômes pathologiques › Processus pathologiques › Caractéristiques de la maladie › Convalescence › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Mélanges complexes › Produits biologiques › Sérums immuns › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Système digestif › Tube digestif › Intestins › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Appareil respiratoire › Poumon › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Fusion membranaire › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Personnes › Tranches d'âge › Adulte › Adulte d'âge moyen › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Phénomènes génétiques › Variation génétique › Mutation › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Tissus › Membranes › Muqueuse › Muqueuse respiratoire › Muqueuse nasale › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Virus › Virus à ARN › Virus à ARN à brin positif › Nidovirales › Coronaviridae › Coronavirus › Betacoronavirus › Virus du SRAS › SARS-CoV-2 › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Peptide hydrolases › Protéases à sérine › Serine endopeptidases › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines virales › Protéines virales structurales › Protéines de l'enveloppe virale › Protéines de fusion virale › Glycoprotéine de spicule des coronavirus › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Techniques d'investigation › Techniques in vitro › Techniques de culture › Techniques de culture de tissus › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Phénomènes microbiologiques › Virulence › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Phénomènes microbiologiques › Phénomènes physiologiques viraux › Pénétration virale › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...
questionsmedicales.fr › Phénomènes microbiologiques › Phénomènes physiologiques viraux › Réplication virale › Altered TMPRSS2 usage by SARS-CoV-2 Omicron...