Structural proteomics, electron cryo-microscopy and structural modeling approaches in bacteria-human protein interactions.
Affinity-purification mass spectrometry
Cross-linking mass spectrometry
Electron cryo-microscopy
Host–pathogen interaction
Molecular modeling
Proteomics
Journal
Medical microbiology and immunology
ISSN: 1432-1831
Titre abrégé: Med Microbiol Immunol
Pays: Germany
ID NLM: 0314524
Informations de publication
Date de publication:
Jun 2020
Jun 2020
Historique:
received:
13
08
2019
accepted:
30
01
2020
pubmed:
20
2
2020
medline:
11
2
2021
entrez:
20
2
2020
Statut:
ppublish
Résumé
A central challenge in infection medicine is to determine the structure and function of host-pathogen protein-protein interactions to understand how these interactions facilitate bacterial adhesion, dissemination and survival. In this review, we focus on proteomics, electron cryo-microscopy and structural modeling to showcase instances where affinity-purification (AP) and cross-linking (XL) mass spectrometry (MS) has advanced our understanding of host-pathogen interactions. We highlight cases where XL-MS in combination with structural modeling has provided insight into the quaternary structure of interspecies protein complexes. We further exemplify how electron cryo-tomography has been used to visualize bacterial-human interactions during attachment and infection. Lastly, we discuss how AP-MS, XL-MS and electron cryo-microscopy and -tomography together with structural modeling approaches can be used in future studies to broaden our knowledge regarding the function, dynamics and evolution of such interactions. This knowledge will be of relevance for future drug and vaccine development programs.
Identifiants
pubmed: 32072248
doi: 10.1007/s00430-020-00663-5
pii: 10.1007/s00430-020-00663-5
pmc: PMC7223518
doi:
Substances chimiques
Bacterial Proteins
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
265-275Subventions
Organisme : H2020 Marie Skłodowska-Curie Actions
ID : 765042
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