Hyaluronic acid capsule modulates M protein-mediated adherence and acts as a ligand for attachment of group A Streptococcus to CD44 on human keratinocytes

The Journal of Clinical Investigation
H M SchragerMichael R Wessels

Abstract

We used wild-type and isogenic mutant strains of group A Streptococcus (GAS) that expressed M protein, capsule, or both to study the function of M protein and the hyaluronic acid capsular polysaccharide in attachment of GAS to human keratinocytes. Types 6 and 24, but not type 18, M protein were found to mediate attachment of GAS to soft palate or skin keratinocytes, but this interaction was prevented by the hyaluronic acid capsule on highly encapsulated, or mucoid, strains. Monoclonal antibody to CD44, the principal hyaluronic acid-binding receptor on keratinocytes, inhibited attachment of both highly encapsulated and poorly encapsulated wild type strains of GAS, but not the attachment of acapsular mutants. Transfection of K562 cells with cDNA encoding human CD44 conferred the capacity to bind each of six wild-type strains of GAS, but not to bind acapsular mutants. Because, in contrast to other potential adhesins, the group A streptococcal capsule is both highly conserved and surface-exposed, it may serve as a universal adhesin for attachment of diverse strains of GAS to keratinocytes of the pharyngeal mucosa and the skin.

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Citations

Jun 22, 1999·Immunologic Research·E R Brandt, M F Good
Jun 19, 2002·Journal of Microbiological Methods·Chad R SethmanMarjorie M Cowan
May 26, 1999·Infectious Disease Clinics of North America·S Sriskandan, J Cohen
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May 29, 2002·Proceedings of the National Academy of Sciences of the United States of America·Nancy P HoeJames M Musser
Mar 21, 2003·Proceedings of the National Academy of Sciences of the United States of America·Ioannis GryllosMichael R Wessels
Mar 30, 2005·Proceedings of the National Academy of Sciences of the United States of America·Anders HåkanssonMichael R Wessels
Jul 5, 2007·Molecular Microbiology·Ioannis GryllosMichael R Wessels

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