1976
DOI: 10.7164/antibiotics.29.1297
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Microbial acetylation of M factor of virginiamycin.

Abstract: The M component of virginiamycin was found to be modified by whole cells or cell-free enzyme preparations of a Staphylococcus aureus strain. It was shown that this reaction proceeds by enzymatic acetylation of the secondary alcoholic function of the molecule, followed by a rapid chemical degradation of the 0-acetylated product.

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Cited by 25 publications
(12 citation statements)
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“…An acetyltransferase that inactivates the A compounds was detected in the lysates of two pristinamycin-resistant staphylococcal isolates (10,22). The gene encoding this enzyme, vat, was recently isolated from a staphylococcal plasmid and sequenced (3).…”
mentioning
confidence: 99%
“…An acetyltransferase that inactivates the A compounds was detected in the lysates of two pristinamycin-resistant staphylococcal isolates (10,22). The gene encoding this enzyme, vat, was recently isolated from a staphylococcal plasmid and sequenced (3).…”
mentioning
confidence: 99%
“…The quinupristin-dalfopristin combination has proved useful in fighting infections produced by dangerous antibiotic-resistant strains of staphylococci or enterococci (14,16,22). Resistance to the class A streptogramins takes place either by active efflux mediated by the gene vga in staphylococci (3) or by inactivation via enzymatic acetylation of the antibiotic (12). This inactivation is catalyzed by streptogramin (virginiamycin) acetyltransferases, the products of sat or vat genes (1,5,23).…”
mentioning
confidence: 99%
“…It functions by binding to the 50 s subunit of the ribosome and inhibiting protein synthesis. Resistance to virginiamycin is associated with enzymes encoded by the genes vat(D) and vat(E) that inactivate the A component of virginiamycin (factor M) by acetylation of the hydroxyl group [10,24,29]. We screened all Lactobacillus isolates for the presence of vat(D) and vat(E).…”
Section: Screening For Antimicrobial Resistance Genesmentioning
confidence: 99%