PDBsum entry 2mpv

Protein binding

PDB id: 2mpv

Contents

Protein chain

145 a.a.

PDB id:

2mpv

Name:

Protein binding

Title:

Structural insight into host recognition and biofilm formation by aggregative adherence fimbriae of enteroaggregative esherichia coli

Structure:

Major fimbrial subunit of aggregative adherence fimbria ii aafa. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: aafa. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

S.J.Matthews,Y.Yang,A.A.Berry,N.Pakharukova,J.A.Garnett,W.Lee,E.Cota, B.Liu,S.Roy,M.Tuittila,J.Marchant,K.G.Inman,F.Ruiz-Perez, I.Mandomando,J.P.Nataro,A.V.Zavialov

Key ref:

A.A.Berry et al. (2014). Structural insight into host recognition by aggregative adherence fimbriae of enteroaggregative Escherichia coli. Plos Pathog, 10, e1004404. PubMed id: 25232738 DOI: 10.1371/journal.ppat.1004404

Date:

04-Jun-14 Release date: 29-Oct-14

Protein chain

O30595  (O30595_ECOLX) -  Major fimbrial subunit of aggregative adherence fimbria II AafA from Escherichia coli

Seq: 160 a.a.

Struc: 145 a.a.

DOI no: 10.1371/journal.ppat.1004404

Plos Pathog 10:e1004404 (2014)

PubMed id: 25232738

Structural insight into host recognition by aggregative adherence fimbriae of enteroaggregative Escherichia coli.

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.

ABSTRACT

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.