Flagellar Cap Protein FliD Mediates Adherence of Atypical Enteropathogenic Escherichia coli to Enterocyte Microvilli

Flagellar Cap Protein FliD Mediates Adherence of Atypical Enteropathogenic Escherichia coli to Enterocyte Microvilli

Author Sampaio, Suely Carlos Ferreira Autor UNIFESP Google Scholar
Luiz, Wilson B. Google Scholar
Vieira, Monica Aparecida Midolli Autor UNIFESP Google Scholar
Ferreira, Rita C. C. Google Scholar
Garcia, Bruna Gil Autor UNIFESP Google Scholar
Sinigaglia-Coimbra, Rita Autor UNIFESP Google Scholar
Sampaio, Jorge L. M. Google Scholar
Ferreira, Luis C. S. Google Scholar
Gomes, Tania Aparecida Tardelli Autor UNIFESP Google Scholar
Abstract The expression of flagella correlates with different aspects of bacterial pathogenicity, ranging from adherence to host cells to activation of inflammatory responses by the innate immune system. In the present study, we investigated the role of flagella in the adherence of an atypical enteropathogenic Escherichia coli (aEPEC) strain (serotype O51: H40) to human enterocytes. Accordingly, isogenic mutants deficient in flagellin (FliC), the flagellar structural subunit

the flagellar cap protein (FliD)

or the MotAB proteins, involved in the control of flagellar motion, were generated and tested for binding to differentiated Caco-2 cells. Binding of the aEPEC strain to enterocytes was significantly impaired in strains with the fliC and fliD genes deleted, both of which could not form flagella on the bacterial surface. A nonmotile but flagellated MotAB mutant also showed impaired adhesion to Caco-2 cells. In accordance with these observations, adhesion of aEPEC strain 1711-4 to Caco-2 cells was drastically reduced after the treatment of Caco-2 cells with purified FliD. In addition, incubation of aEPEC bacteria with specific anti-FliD serum impaired binding to Caco-2 cells. Finally, incubation of Caco-2 cells with purified FliD, followed by immunolabeling, showed that the protein was specifically bound to the microvillus tips of differentiated Caco-2 cells. The aEPEC FliD or anti-FliD serum also reduced the adherence of prototype typical enteropathogenic, enterohemorrhagic, and enterotoxigenic E. coli strains to Caco-2 cells. In conclusion, our findings further strengthened the role of flagella in the adherence of aEPEC to human enterocytes and disclosed the relevant structural and functional involvement of FliD in the adhesion process.
xmlui.dri2xhtml.METS-1.0.item-coverage Washington
Language English
Sponsor Sao Paulo Research Foundation (FAPESP)
Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
Grant number FAPESP: 2011/12664-5
FAPESP: 2009/50399-1
CNPq: 150833/2012-1
Date 2016
Published in Infection And Immunity. Washington, v. 84, n. 4, p. 1112-1122, 2016.
ISSN 0019-9567 (Sherpa/Romeo, impact factor)
Publisher Amer Soc Microbiology
Extent 1112-1122
Origin http://dx.doi.org/10.1128/IAI.01001-15
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000377103600023
URI https://repositorio.unifesp.br/handle/11600/56093

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