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PROSITE documentation PDOC51223

MAP repeat profile





Description

Map (MHC class II analogous protein), also known as eap (extracellular adherence protein) and p70, is exclusively found in Staphylococcus aureus. It is a cell-wall associated protein, which is capable of binding to a number of different extracellular matrix glycoploteins and plasma proteins, and to the cell surface of Staphylococcus aureus. Besides the broad binding specificity, map has been shown to be important in the adherence to and internalization of Staphylococcus aureus by eukaryotic cells as well as being capable of modulating inflammatory response through its interactions with ICAM-1 (intercellular adhesion molecule-1), although its biological role in vivo remains to date unclear [1].

The protein consists of a signal peptide followed by a unique sequence of about 20 amino acids and four to six repeated MAP domains of 110-amino acid residues. Within each repeat there is a subdomain consisting of 31 residues that was found to be highly homologous to the N-terminal β-chain of many MHC class II molecules [2].

The crystal structure of the MAP domain has been solved (see <PDB:1YN3>) and shows a core fold that is comprised of an α-helix lying diagonally across a five-stranded, mixed β-sheet. This structure is very similar to the C-terminal domain of bacterial superantigens [3].

The profile we developed covers the entire MAP repeat.

Note:

MAP repeats have been found in all but 5 of 140 Staphylococcus aureus strains examined, but they were not detected in reference strains or clinical isolates of Staphylococcus epidermidis [1].

Last update:

June 2006 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

MAP, PS51223; MAP repeat profile  (MATRIX)


References

1AuthorsHarraghy N. Hussain M. Haggar A. Chavakis T. Sinha B. Herrmann M. Flock J.I.
TitleThe adhesive and immunomodulating properties of the multifunctional Staphylococcus aureus protein Eap.
SourceMicrobiology 149:2701-2707(2003).
PubMed ID14523103

2AuthorsJonsson K. McDevitt D. McGavin M.H. Patti J.M. Hook M.
TitleStaphylococcus aureus expresses a major histocompatibility complex class II analog.
SourceJ. Biol. Chem. 270:21457-21460(1995).
PubMed ID7545162

3AuthorsGeisbrecht B.V. Hamaoka B.Y. Perman B. Zemla A. Leahy D.J.
TitleThe crystal structures of EAP domains from Staphylococcus aureus reveal an unexpected homology to bacterial superantigens.
SourceJ. Biol. Chem. 280:17243-17250(2005).
PubMed ID15691839
DOI10.1074/jbc.M412311200



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