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Structural and functional studies of Escherichia coli Aggregative Adherence Fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding

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Title: Structural and functional studies of Escherichia coli Aggregative Adherence Fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding
Authors: Jønsson, R
Liu, B
Struve, C
Yang, Y
Jenssen, H
Krogfelt, K
Matthews, SJ
Item Type: Journal Article
Abstract: Enteroaggregative Escherichia coli (EAEC) is an emerging cause of acute and persistent diarrhea worldwide. The pathogenesis of different EAEC stains is complicated, however, the early essential step begins with attachment of EAEC to intestinal mucosa via aggregative adherence fimbriae (AAFs). Currently, five different variants have been identified, which all share a degree of similarity in the gene organization of their operons and sequences. Here, we report the solution structure of Agg5A from the AAF/V variant. While preserving the major structural features shared by all AAF members, only Agg5A possesses an inserted helix at the beginning of the donor strand, which together with altered surface electrostatics, renders the protein unable to interact with fibronectin. Hence, here we characterize the first AAF variant with a binding mode that varies from previously described AAFs
Issue Date: 9-Dec-2016
Date of Acceptance: 1-Dec-2016
URI: http://hdl.handle.net/10044/1/42957
DOI: https://dx.doi.org/10.1016/j.bbapap.2016.11.017
ISSN: 1570-9639
Publisher: Elsevier
Start Page: 304
End Page: 311
Journal / Book Title: BBA Protein and Proteomics
Volume: 1865
Issue: 3
Copyright Statement: © 2016 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Sponsor/Funder: Medical Research Council (MRC)
Wellcome Trust
Wellcome Trust
Wellcome Trust
Funder's Grant Number: MR/J006874/1B
100280/Z/12/Z
WT/104933/z/14/z
202926/Z/16/Z
Keywords: Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Biophysics
Aggregative adherence fimbriae
Agg5A
Chaperone-usher
Pilin
Donor strand complementation
E. coli
Fibronectin
PERSISTENT DIARRHEA
CRYSTAL-STRUCTURE
VIRULENCE GENES
STRAINS
FAMILY
PILUS
ASSIGNMENT
TRAVELERS
OUTBREAK
CHILDREN
06 Biological Sciences
02 Physical Sciences
Publication Status: Published
Open Access location: http://10.0.3.248/j.bbapap.2016.11.017
Appears in Collections:Faculty of Natural Sciences