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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.)

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

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Author(s):
Sampaio, Suely C. F. [1, 2] ; Luiz, Wilson B. [3, 4] ; Vieira, Monica A. M. [1] ; Ferreira, Rita C. C. [3, 5] ; Garcia, Bruna G. [1] ; Sinigaglia-Coimbra, Rita ; Sampaio, Jorge L. M. [6, 7] ; Ferreira, Luis C. S. [3] ; Gomes, Tania A. T. [1]
Total Authors: 9
Affiliation:
[1] Univ Fed Sao Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, Sao Paulo - Brazil
[2] Fac Ciencias Med Santa Casa Sao Paulo, Dept Patol, Div Microbiol, Sao Paulo - Brazil
[3] Univ Sao Paulo, Inst Ciencias Biomed, Dept Microbiol, BR-05508 Sao Paulo - Brazil
[4] Univ Estadual Santa Cruz, Ctr Biotecnol & Genet, Ilheus, Bahia - Brazil
[5] Univ Fed Sao Paulo, Escola Paulista Med, Ctr Microscopia Eletron, Sao Paulo - Brazil
[6] Univ Sao Paulo, Fac Ciencias Farmaceut, Sao Paulo - Brazil
[7] Inst Fleury Ensino & Pesquisa, Sao Paulo - Brazil
Total Affiliations: 7
Document type: Journal article
Source: Infection and Immunity; v. 84, n. 4, p. 1112-1122, APR 2016.
Web of Science Citations: 6
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. (AU)

FAPESP's process: 11/12664-5 - Exploring the interactions of Enteropathogenic Escherichia coli with intestinal cells in vitro and in vivo
Grantee:Tânia Aparecida Tardelli Gomes do Amaral
Support Opportunities: Regular Research Grants