Serotype F double‐ and triple‐converting phage insertionally inactivate the Staphylococcus aureus β‐toxin determinant by a common molecular mechanism

The precise molecular mechanism of Staphylococcus aureus β‐toxin inactivation by the serotype F triple‐converting phage φ42, φA1 and φA3 was investigated. Sequence analysis of the φ42 (attP) and Staphylococcus aureus (attB) attachment sites and the left (attL) and right (attR) chromosomal/bacterioph...

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Veröffentlicht in:FEMS microbiology letters 1993-01, Vol.106 (2), p.147-155
Hauptverfasser: Carroll, J.D., Cafferkey, M.T., Coleman, D.C.
Format: Artikel
Sprache:eng
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Zusammenfassung:The precise molecular mechanism of Staphylococcus aureus β‐toxin inactivation by the serotype F triple‐converting phage φ42, φA1 and φA3 was investigated. Sequence analysis of the φ42 (attP) and Staphylococcus aureus (attB) attachment sites and the left (attL) and right (attR) chromosomal/bacteriophage DNA junctions of individual lysogens, each harbouring a triple‐converting phage, revealed the presence of a common 14‐bp core sequence in all four sites. These findings indicate that the genomes of the triple‐converting phage integrate into the 5′‐end of the β‐toxin gene (hlb) by a site‐ and orientation‐specific mechanism identical to that previously described for the serotype F double‐converting phage φ13.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1993.tb05951.x