Publication Date:
1995-04-07
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneewind, O -- Fowler, A -- Faull, K F -- AI 33985/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 7;268(5207):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California School of Medicine, Los Angeles 90024, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701329" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Bacterial Proteins/*chemistry
;
Base Sequence
;
Carrier Proteins/chemistry
;
Cell Wall/*chemistry
;
Chromatography, Affinity
;
Chromatography, High Pressure Liquid/methods
;
Electrophoresis, Polyacrylamide Gel
;
Maltose-Binding Proteins
;
Membrane Proteins/*chemistry
;
Molecular Sequence Data
;
Recombinant Fusion Proteins/chemistry
;
Staphylococcal Protein A/chemistry
;
Staphylococcus aureus/*chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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