Structure of the UspA1 protein fragment from Moraxella catarrhalis responsible for C3d binding.


Journal

Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206

Informations de publication

Date de publication:
01 11 2019
Historique:
received: 07 03 2019
revised: 03 08 2019
accepted: 05 08 2019
pubmed: 11 8 2019
medline: 23 6 2020
entrez: 11 8 2019
Statut: ppublish

Résumé

The gram-negative bacterium Moraxella catarrhalis infects humans exclusively, causing various respiratory tract diseases, including acute otitis media in children, septicaemia or meningitis in adults, and pneumonia in the elderly. To do so, M. catarrhalis expresses virulence factors facilitating its entry and survival in the host. Among them are the ubiquitous surface proteins (Usps): A1, A2, and A2H, which all belong to the trimeric autotransporter adhesin family. They bind extracellular matrix molecules and inhibit the classical and alternative pathways of the complement cascade by recruiting complement regulators C3d and C4b binding protein. Here, we report the 2.5 Å resolution X-ray structure of UspA1

Identifiants

pubmed: 31400508
pii: S1047-8477(19)30172-8
doi: 10.1016/j.jsb.2019.08.002
pmc: PMC6839023
pii:
doi:

Substances chimiques

Bacterial Outer Membrane Proteins 0
UspA protein, Moraxella catarrhalis 0
Complement C3d 80295-45-0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

77-85

Subventions

Organisme : Wellcome Trust
Pays : United Kingdom

Informations de copyright

Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.

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Auteurs

Kornelia M Mikula (KM)

Molecular and Integrative Biosciences, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.

Robert Kolodziejczyk (R)

Molecular and Integrative Biosciences, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.

Adrian Goldman (A)

Molecular and Integrative Biosciences, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland; Astbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds, UK. Electronic address: a.goldman@leeds.ac.uk.

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Classifications MeSH