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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectin

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Moraes, Claudia T. P. [1] ; Polatto, Juliana M. [1] ; Rossato, Sarita S. [1] ; Izquierdo, Mariana [2] ; Munhoz, Danielle D. [1] ; Martins, Fernando H. [1] ; Pimenta, Daniel C. [3] ; Farfan, Mauricio J. [2] ; Elias, Waldir P. [1] ; Barbosa, Angela S. [1] ; Piazza, Roxane M. F. [1]
Total Authors: 11
[1] Inst Butantan, Lab Bacteriol, BR-05503900 Sao Paulo, SP - Brazil
[2] Univ Chile, Ctr Estudios Mol, Dept Pediat, Hosp Dr Luis Calvo Mackenna, Santiago - Chile
[3] Inst Butantan, Lab Bioquim & Biofis, BR-05503900 Sao Paulo, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: BMC Microbiology; v. 15, DEC 18 2015.
Web of Science Citations: 6

Background: Enteropathogenic Escherichia coli (EPEC) is distinguished mainly by the presence of EPEC adherence factor plasmid (pEAF) in typical EPEC (tEPEC) and its absence in atypical EPEC (aEPEC). The initial adherence to the intestinal mucosa is complex and mediated by adhesins other than bundle-forming pilus, which is not produced by aEPEC. Extracellular matrix (ECM) proteins of eukaryotic cells are commonly recognized by bacterial adhesins. Therefore, binding to ECM proteins may facilitate colonization, invasion and/or signaling by intestinal pathogens. Previous studies from our group demonstrated that aEPEC O26:H11 (strain BA2103) showed high binding activity to fibronectin, not shared by its counterpart, aEPEC O26:HNM. Results: In the present study, using mass spectrometry after fibronectin-associated immunoprecipitation, two proteins, flagellin (50 kDa) and GroEL (52 kDa), were identified and BA2103 binding ability to fibronectin was inhibited in the presence of anti-H11 and anti-GroEL sera, but not by either naive rabbit or other unrelated sera. It was also observed that the presence of purified flagellin inhibits adhesion of BA2103 to cellular fibronectin in a dose-dependent manner. Additionally, BA2103 GroEL is similar to the same protein of uropathogenic E. coli. Conclusions: Our results suggest that flagellin may play a role in the in vitro interaction of BA2103 with cellular fibronectin, and GroEL can be an accessory protein in this process. (AU)

FAPESP's process: 04/12136-5 - Atypical enteropathogenetic Escherichia coli (atypical EPEC)
Grantee:Waldir Pereira Elias Junior
Support type: Research Projects - Thematic Grants