RESUMO
Shigella flexneri type Y strains (-;3,4) are converted to type X (-;7,8) by bacteriophage X (SFX) that causes glucosylation of the O-antigenic polysaccharide chain. The gene (gtr) encoding glucosyl transferase from bacteriophage X has been cloned and sequenced. The protein encoded by gtr consists of 416 amino acids with a M(r) of 47,369. The cloned gtr product was able to convert a S. flexneri strain type Y (SFL 124, a live attenuated candidate vaccine strain) to type X. The importance of the hybrid strain in vaccine development is discussed.
Assuntos
Bacteriófagos/genética , Genes Virais , Glucosiltransferases/genética , Shigella flexneri/genética , Proteínas Estruturais Virais/genética , Sequência de Aminoácidos , Bacteriófagos/enzimologia , Sequência de Bases , Sequência de Carboidratos , Clonagem Molecular , Dados de Sequência Molecular , Polissacarídeos Bacterianos/biossínteseRESUMO
Bacteriophage SF6 antigenically converts Shigella flexneri serotype Y strains (-;3,4) to type 3b carrying group antigen 6,3,4 by means of an O-acetylation of the O-antigenic polysaccharide chain. The gene for O-acetyl transferase of bacteriophage SF6 has been cloned, identified and sequenced. The predicted O-acetyl transferase protein encoded by this gene was found to consist of 333 amino acids, (37,185 daltons) and to have some similarity with the galactose-1-phosphate uridylyltransferase protein of Escherichia coli. The gene has been shown to function in a live vaccine strain of S. flexneri Y type (delta aroD), making it a 3b type. The converted type 3b strain, SFL1104, was found to elicit significant protection against challenge by both wild-type serotypes 3b and Y in a guinea-pig keratoconjunctivitis model.