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. 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.
Schneewind
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O
Department of Microbiology and Immunology, University of California School of Medicine, Los Angeles 90024, USA.
Fowler
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A
Faull
K F
KF
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001483:Base Sequence; D002352:Carrier Proteins / Q000737:chemistry; D002473:Cell Wall / Q000737:chemistry*; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D058619:Maltose-Binding Proteins; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D013205:Staphylococcal Protein A / Q000737:chemistry; D013211:Staphylococcus aureus / Q000737:chemistry*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D008565:Membrane Proteins; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A