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Science 7 April 1995:
Vol. 268. no. 5207, pp. 103 - 106
DOI: 10.1126/science.7701329

Articles

Science, Vol 268, Issue 5207, 103-106
Copyright © 1995 by American Association for the Advancement of Science


articles

Structure of the cell wall anchor of surface proteins in Staphylococcus aureus

O Schneewind, A Fowler, and KF Faull

Department of Microbiology and Immunology, University of California School of Medicine, Los Angeles 90024, USA.

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.


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Introduction of the mec Element (Methicillin Resistance) into Staphylococcus aureus Alters In Vitro Functional Activities of Fibrinogen and Fibronectin Adhesins.
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A Monoclonal Antibody Enhances Ligand Binding of Fibronectin MSCRAMM (Adhesin) from Streptococcus dysgalactiae.
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Protein SIC, a Novel Extracellular Protein of Streptococcus pyogenes Interfering with Complement Function.
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Identification of Residues in the Staphylococcus aureus Fibrinogen-binding MSCRAMM Clumping Factor A (ClfA) That Are Important for Ligand Binding.
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Loss of Clumping Factor B Fibrinogen Binding Activity by Staphylococcus aureus Involves Cessation of Transcription, Shedding and Cleavage by Metalloprotease.
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Anchoring of Surface Proteins to the Cell Wall of Staphylococcus aureus. CYSTEINE 184 AND HISTIDINE 120 OF SORTASE FORM A THIOLATE-IMIDAZOLIUM ION PAIR FOR CATALYSIS.
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