The immune evasion protein Sbi of Staphylococcus aureus occurs both extracellularly and anchored to the cell envelope by binding lipoteichoic acid

Summary The Sbi protein of Staphylococcus aureus comprises two IgG‐binding domains similar to those of protein A and a region that triggers the activation of complement C3. Sbi is expressed on the cell surface but its C‐terminal domain lacks motifs associated with wall or membrane anchoring of prote...

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Published inMolecular microbiology Vol. 83; no. 4; pp. 789 - 804
Main Authors Smith, Emma Jane, Corrigan, Rebecca M., van der Sluis, Tetje, Gründling, Angelika, Speziale, Pietro, Geoghegan, Joan A., Foster, Timothy J.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.02.2012
Blackwell
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Summary:Summary The Sbi protein of Staphylococcus aureus comprises two IgG‐binding domains similar to those of protein A and a region that triggers the activation of complement C3. Sbi is expressed on the cell surface but its C‐terminal domain lacks motifs associated with wall or membrane anchoring of proteins in Gram‐positive bacteria. Cell‐associated Sbi fractionates with the cytoplasmic membrane and is not solubilized during protoplast formation. S. aureus expressing Sbi truncates of the C‐terminal Y domain allowed identification of residues that are required for association of Sbi with the membrane. Recombinant Sbi bound to purified cytoplasmic membrane material in vitro and to purified lipoteichoic acid. This explains how Sbi partitions with the membrane in fractionation experiments yet is partially exposed on the cell surface. An LTA‐defective mutant of S. aureus had reduced levels of Sbi in the cytoplasmic membrane.
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ArticleID:MMI7966
ark:/67375/WNG-D4PPHWB8-X
istex:6C40E267A52738E495654F06601F36A3A65B7E21
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Present address: Department of Immunohematology and Blood Transfusion, Leiden University Medical Center, Albinusdreef 2, 2333 ZA, Leiden, the Netherlands.
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Re-use of this article is permitted in accordance with the Terms and Conditions set out at http://wileyonlinelibrary.com/onlineopen#OnlineOpen_Terms
ISSN:0950-382X
1365-2958
DOI:10.1111/j.1365-2958.2011.07966.x