Dear Spiral user, We’re pleased to introduce Helix, https://helix.imperial.ac.uk/ Imperial’s new repository for research datasets. Please use Helix for all future dataset deposits. There is no change to Spiral - continue depositing as usual. For queries, contact the Research Data Management team at rdm-enquiries@imperial.ac.uk. Kind regards, the Spiral Team. The Spiral team
Structural and functional studies of Escherichia coli Aggregative Adherence Fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding
File(s)
OA Location
Author(s)
Jønsson, R
Liu, B
Struve, C
Yang, Y
Jenssen, H
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
Date Issued
2016-12-09
Date Acceptance
2016-12-01
Citation
BBA Protein and Proteomics, 2016, 1865 (3), pp.304-311
URI
DOI
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
Medical Research Council (MRC)
Wellcome Trust
Wellcome Trust
Wellcome Trust
Grant Number
MR/J006874/1B
100280/Z/12/Z
WT/104933/z/14/z
202926/Z/16/Z
Subjects
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