This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bergonzelli, G. E. Articles by Corthésy-Theulaz, I. E. Search for Related Content PubMed PubMed Citation Articles by Bergonzelli, G. E. Articles by Corthésy-Theulaz, I. E.

GroEL of Lactobacillus johnsonii La1 (NCC 533) Is Cell Surface Associated: Potential Role in Interactions with the Host and the Gastric Pathogen Helicobacter pylori

Nestlé Research Center, CH-1000 Lausanne 26, Switzerland

Received 24 March 2005/ Returned for modification 31 May 2005/ Accepted 13 October 2005

Heat shock proteins of the GroEL or Hsp60 class are highly conserved proteins essential to all living organisms. Even though GroEL proteins are classically considered intracellular proteins, they have been found at the surface of several mucosal pathogens and have been implicated in cell attachment and immune modulation. The purpose of the present study was to investigate the GroEL protein of a gram-positive probiotic bacterium, Lactobacillus johnsonii La1 (NCC 533). Its presence at the bacterial surface was demonstrated using a whole-cell enzyme-linked immunosorbent assay and could be detected in bacterial spent culture medium by immunoblotting. To assess binding of La1 GroEL to mucins and intestinal epithelial cells, the La1 GroEL protein was expressed in Escherichia coli. We report here that La1 recombinant GroEL (rGroEL) binds to mucins and epithelial cells and that this binding is pH dependent. Immunomodulation studies showed that La1 rGroEL stimulates interleukin-8 secretion in macrophages and HT29 cells in a CD14-dependent mechanism. This property is common to rGroEL from other gram-positive bacteria but not to the rGroEL of the gastric pathogen Helicobacter pylori. In addition, La1 rGroEL mediates the aggregation of H. pylori but not that of other intestinal pathogens. Our in vitro results suggest that GroEL proteins from La1 and other lactic acid bacteria might play a role in gastrointestinal homeostasis due to their ability to bind to components of the gastrointestinal mucosa and to aggregate H. pylori.

Editor: J. D. Clements

This article has been cited by other articles:

• Anwar, M. A., Kralj, S., van der Maarel, M. J. E. C., Dijkhuizen, L. (2008). The Probiotic Lactobacillus johnsonii NCC 533 Produces High-Molecular-Mass Inulin from Sucrose by Using an Inulosucrase Enzyme. Appl. Environ. Microbiol. 74: 3426-3433 [Abstract] [Full Text]  
• Wuppermann, F. N., Molleken, K., Julien, M., Jantos, C. A., Hegemann, J. H. (2008). Chlamydia pneumoniae GroEL1 Protein Is Cell Surface Associated and Required for Infection of HEp-2 Cells. J. Bacteriol. 190: 3757-3767 [Abstract] [Full Text]  
• Aly, K. A., Krall, L., Lottspeich, F., Baron, C. (2008). The Type IV Secretion System Component VirB5 Binds to the trans-Zeatin Biosynthetic Enzyme Tzs and Enables Its Translocation to the Cell Surface of Agrobacterium tumefaciens. J. Bacteriol. 190: 1595-1604 [Abstract] [Full Text]  
• Ikeda, R., Saito, F., Matsuo, M., Kurokawa, K., Sekimizu, K., Yamaguchi, M., Kawamoto, S. (2007). Contribution of the Mannan Backbone of Cryptococcal Glucuronoxylomannan and a Glycolytic Enzyme of Staphylococcus aureus to Contact-Mediated Killing of Cryptococcus neoformans. J. Bacteriol. 189: 4815-4826 [Abstract] [Full Text]  
• Hurmalainen, V., Edelman, S., Antikainen, J., Baumann, M., Lahteenmaki, K., Korhonen, T. K. (2007). Extracellular proteins of Lactobacillus crispatus enhance activation of human plasminogen. Microbiology 153: 1112-1122 [Abstract] [Full Text]