Surface glycosaminoglycans mediate adherence between HeLa cells and Lactobacillus salivarius Lv72

BMC Microbiology

Research Article

Rebeca Martín¹  Susana Escobedo¹  Carla Martín¹  Juan E Suárez²  Luis M Quirós³ 

[1] Área de Microbiología, Universidad de Oviedo, Julián Clavería 6, 33006, Oviedo, Spain;Instituto Universitario de Biotecnología, Universidad de Oviedo, Oviedo, Spain;Área de Microbiología, Universidad de Oviedo, Julián Clavería 6, 33006, Oviedo, Spain;Instituto Universitario de Biotecnología, Universidad de Oviedo, Oviedo, Spain;Instituto de Productos Lacteos de Asturias (IPLA-CSIC), Villaviciosa, Spain;Área de Microbiología, Universidad de Oviedo, Julián Clavería 6, 33006, Oviedo, Spain;Instituto Univesitario de Oncología del Principado de Asturias (IUOPA), Universidad de Oviedo, Oviedo, Spain;

关键词: Proteoglycans;    Glycosaminoglycans;    Lactobacillus;    Epithelial cell cultures;   

DOI  :  10.1186/1471-2180-13-210

 received in 2013-03-23, accepted in 2013-09-11,  发布年份 2013

来源: Springer

【 摘 要 】

BackgroundThe adhesion of lactobacilli to the vaginal surface is of paramount importance to develop their probiotic functions. For this reason, the role of HeLa cell surface proteoglycans in the attachment of Lactobacillus salivarius Lv72, a mutualistic strain of vaginal origin, was investigated.ResultsIncubation of cultures with a variety of glycosaminoglycans (chondroitin sulfate A and C, heparin and heparan sulfate) resulted in marked binding interference. However, no single glycosaminoglycan was able to completely abolish cell binding, the sum of all having an additive effect that suggests cooperation between them and recognition of specific adhesins on the bacterial surface. In contrast, chondroitin sulfate B enhanced cell to cell attachment, showing the relevance of the stereochemistry of the uronic acid and the sulfation pattern on binding. Elimination of the HeLa surface glycosaminoglycans with lyases also resulted in severe adherence impairment. Advantage was taken of the Lactobacillus-glycosaminoglycans interaction to identify an adhesin from the bacterial surface. This protein, identify as a soluble binding protein of an ABC transporter system (OppA) by MALDI-TOF/(MS), was overproduced in Escherichia coli, purified and shown to interfere with L. salivarius Lv72 adhesion to HeLa cells.ConclusionsThese data suggest that glycosaminoglycans play a fundamental role in attachment of mutualistic bacteria to the epithelium that lines the cavities where the normal microbiota thrives, OppA being a bacterial adhesin involved in the process.

【 授权许可】

Unknown   
© Martín et al.; licensee BioMed Central Ltd. 2013. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.