Molecular analysis of lytic genes of bacteriophage 80α ofStaphylococcus aureus

Abstract

Nucleotide sequencing of a 3779-bp fragment of the Staphylococcus aureus bacteriophage 80α revealed two open reading frames: ORF1, designated as lytA, which encodes a polypeptide of 481 amino acids with an apparent Mrof 53.81 kDa; and ORF2, designated as holin, which encodes for a hydrophobic polypeptide of 145 amino acids with an apparent Mrof 15.58 kDa and exhibits two putative transmembrane helices. Both genes showed 100% sequence homology to that of the peptidoglycan hydrolase and holin genes of the S. aureus phage [Formula: see text] reported earlier. In addition, the downstream sequences of the lytA gene were homologous to the phage attachment site (attP) of the phage [Formula: see text]. Based on our data we propose that the lytic system of the phage 80α evolved from that of phage [Formula: see text].Key words: attachment site, bacteriophage 80α, holin, peptidoglycan hydrolase, Staphylococcus aureus.