Surface-Exposed Histone-Like Protein A Modulates Adherence of Streptococcus gallolyticus to Colon Adenocarcinoma Cells

Author:

Boleij Annemarie1,Schaeps Renée M. J.1,de Kleijn Stan12,Hermans Peter W.2,Glaser Philippe3,Pancholi Vijay4,Swinkels Dorine W.1,Tjalsma Harold1

Affiliation:

1. Department of Laboratory Medicine, Clinical Chemistry

2. Laboratory of Pediatric Infectious Diseases, Nijmegen Institutes for Infection, Inflammation and Immunity and Oncology of the Radboud University Nijmegen Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands

3. Unité de Génomique des Microorganismes Pathogènes, Institut Pasteur, 28 Rue du Dr. Roux, 75724 Paris Cedex 15, France

4. Laboratory of Bacterial Pathogenesis, Department of Pathology, Ohio State University College of Medicine and Public Health, 288A, Tzgournis Medical Research Facility, 420 W. 12th Avenue, Columbus, Ohio 43210-1214

Abstract

ABSTRACT Streptococcus gallolyticus (formerly known as Streptococcus bovis biotype I) is a low-grade opportunistic pathogen which is considered to be associated with colon cancer. It is thought that colon polyps or tumors are the main portal of entry for this bacterium and that heparan sulfate proteoglycans (HSPGs) at the colon tumor cell surface are involved in bacterial adherence during the first stages of infection. In this study, we have shown that the histone-like protein A (HlpA) of S. gallolyticus is a genuine anchorless bacterial surface protein that binds to lipoteichoic acid (LTA) of the gram-positive cell wall in a growth phase-dependent manner. In addition, HlpA was shown to be one of the major heparin-binding proteins of S. gallolyticus able to bind to the HSPG-expressing colon tumor cell lines HCT116 and HT-29. Strikingly, although wild-type levels of HlpA appeared to contribute to adherence, coating of additional HlpA at the bacterial surface resulted in reduced binding to colon tumor cells. This may be explained by the fact that heparan sulfate and LTA compete for the same binding site in HlpA. Altogether, this study implies that HlpA serves as a fine-tuning factor for bacterial adherence.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

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