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Microbiology 149 (2003), 2701-2707; DOI  10.1099/mic.0.26465-0
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Microbiology 149 (2003), 2701-2707; DOI  10.1099/mic.0.26465-0
© 2003 Society for General Microbiology

The adhesive and immunomodulating properties of the multifunctional Staphylococcus aureus protein Eap

Niamh Harraghy1, Muzaffar Hussain2, Axana Haggar3, Triantafyllos Chavakis4, Bhanu Sinha2, Mathias Herrmann1 and Jan-Ingmar Flock3

1 Institute of Medical Microbiology and Hygiene, University of Saarland Hospital, D-66421 Homburg/Saar, Germany
2 Institute of Microbiology, University Hospital of Muenster, D-48149 Muenster, Germany
3 Department of Laboratory Medicine, Karolinska Institutet, Huddinge University Hospital, S-141 86 Huddinge, Sweden
4 Department of Medicine 1, University Hospital Heidelberg, D-69115 Heidelberg, Germany

Correspondence
Mathias Herrmann
mathias.herrmann{at}uniklinik-saarland.de

Adherence of Staphylococcus aureus to the host tissue is an important step in the initiation of pathogenesis. At least 10 adhesins produced by S. aureus have been described and it is becoming clear that the expression of these adhesins and their interactions with eukaryotic cells involve complex processes. Some of these, such as the fibronectin-binding proteins (FnBPs) and Clumping Factor A, are well characterized. However, in the last 10 years a number of novel S. aureus adhesins have been described. Functional analyses of these proteins, one of which is Eap (extracellular adherence protein, also known as Map and p70), are revealing important information on the pathogenesis of staphylococcal disease. More than 10 years after the first report of Eap, we are beginning to understand that this protein, which has a broad spectrum of functions, may be a critical factor in the pathogenesis of S. aureus. This review will focus on the interactions of Eap with eukaryotic cells, plasma proteins and the extracellular matrix as well as on the recently recognized role of Eap as an important mediator in the immune response to staphylococcal infection.




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