Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 45, Pages -Publisher
ELSEVIER
DOI: 10.1074/jbc.M112.376434
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Funding
- Medical Faculty of the University of Rostock
- German Federal Ministry of Education and Research (BMBF)
- Health Research Council of New Zealand
- Tertiary Education Commission of New Zealand
- Maurice Wilkins Centre for Molecular Biodiscovery
- National Health and Medical Research Council of Australia
- New Zealand International Doctoral Research Scholarship (Education New Zealand)
- Australian Research Council Federation Fellowship
- National Health and Medical Research Council of Australia Principal Research Fellowship
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Streptococcus pyogenes is an exclusively human pathogen. Streptococcal attachment to and entry into epithelial cells is a prerequisite for a successful infection of the human host and requires adhesins. Here, we demonstrate that the multidomain protein Epf from S. pyogenes serotype M49 is a streptococcal adhesin. An epf-deficient mutant showed significantly decreased adhesion to and internalization into human keratinocytes. Cell adhesion is mediated by the N-terminal domain of Epf (EpfN) and increased by the human plasma protein plasminogen. The crystal structure of EpfN, solved at 1.6 angstrom resolution, shows that it consists of two subdomains: a carbohydrate-binding module and a fibronectin type III domain. Both fold types commonly participate in ligand receptor and protein-protein interactions. EpfN is followed by 18 repeats of a domain classified as DUF1542 (domain of unknown function 1542) and a C-terminal cell wall sorting signal. The DUF1542 repeats are not involved in adhesion, but biophysical studies show they are predominantly alpha-helical and form a fiber-like stalk of tandem DUF1542 domains. Epf thus conforms with the widespread family of adhesins known as MSCRAMMs (microbial surface components recognizing adhesive matrix molecules), in which a cell wall-attached stalk enables long range interactions via its adhesive N-terminal domain.
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