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Structure of the Cell Wall Anchor of Surface Proteins in Staphylococcus aureus

Many surface proteins are anchored to the cell wall of Gram-positive bacteria and are involved in the pathogenesis of these organisms. A hybrid molecule was designed that, when expressed in Staphylococcus aureus, was anchored to the cell wall and could be released by controlled enzymatic digestion....

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1995-04, Vol.268 (5207), p.103-106
Main Authors: Schneewind, Olaf, Fowler, Audree, Faull, Kym F.
Format: Article
Language:English
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Summary:Many surface proteins are anchored to the cell wall of Gram-positive bacteria and are involved in the pathogenesis of these organisms. A hybrid molecule was designed that, when expressed in Staphylococcus aureus, was anchored to the cell wall and could be released by controlled enzymatic digestion. By a combination of molecular biology and mass spectrometry techniques, the structure of the cell wall anchor of surface proteins in S. aureus was revealed. After cleavage of surface proteins between threonine and glycine of the conserved LPXTG motif, the carboxyl of threonine is amide-linked to the free amino group of the pentaglycine crossbridge in the staphylococcal cell wall.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.7701329