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PDBsum entry 2mpv
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Protein binding
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PDB id
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2mpv
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References listed in PDB file
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Key reference
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Title
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Structural insight into host recognition by aggregative adherence fimbriae of enteroaggregative escherichia coli.
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Authors
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A.A.Berry,
Y.Yang,
N.Pakharukova,
J.A.Garnett,
W.C.Lee,
E.Cota,
J.Marchant,
S.Roy,
M.Tuittila,
B.Liu,
K.G.Inman,
F.Ruiz-Perez,
I.Mandomando,
J.P.Nataro,
A.V.Zavialov,
S.Matthews.
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Ref.
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Plos Pathog, 2014,
10,
e1004404.
[DOI no: ]
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PubMed id
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Abstract
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Enteroaggregative Escherichia coli (EAEC) is a leading cause of acute and
persistent diarrhea worldwide. A recently emerged Shiga-toxin-producing strain
of EAEC resulted in significant mortality and morbidity due to progressive
development of hemolytic-uremic syndrome. The attachment of EAEC to the human
intestinal mucosa is mediated by aggregative adherence fimbria (AAF). Using
X-ray crystallography and NMR structures, we present new atomic resolution
insight into the structure of AAF variant I from the strain that caused the
deadly outbreak in Germany in 2011, and AAF variant II from archetype strain
042, and propose a mechanism for AAF-mediated adhesion and biofilm formation.
Our work shows that major subunits of AAF assemble into linear polymers by donor
strand complementation where a single minor subunit is inserted at the tip of
the polymer by accepting the donor strand from the terminal major subunit.
Whereas the minor subunits of AAF have a distinct conserved structure, AAF major
subunits display large structural differences, affecting the overall pilus
architecture. These structures suggest a mechanism for AAF-mediated adhesion and
biofilm formation. Binding experiments using wild type and mutant subunits (NMR
and SPR) and bacteria (ELISA) revealed that despite the structural differences
AAF recognize a common receptor, fibronectin, by employing clusters of basic
residues at the junction between subunits in the pilus. We show that
AAF-fibronectin attachment is based primarily on electrostatic interactions, a
mechanism not reported previously for bacterial adhesion to biotic surfaces.
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