PMID- 2533245 OWN - NLM STAT- MEDLINE DCOM- 19900308 LR - 20061115 IS - 0022-1287 (Print) IS - 0022-1287 (Linking) VI - 135 IP - 6 DP - 1989 Jun TI - Staphylococcus aureus bacteriophages mediating the simultaneous lysogenic conversion of beta-lysin, staphylokinase and enterotoxin A: molecular mechanism of triple conversion. PG - 1679-97 AB - A new group of serotype F bacteriophages of Staphylococcus aureus has been found which mediates the simultaneous triple-lysogenic conversion of enterotoxin A, staphylokinase and beta-lysin. The phages were recovered fro methicillin-resistant strains of S. aureus isolated in Irish hospitals between 1971 and 1988 and from strain PS42-D, which has been used as the propagating strain for the S. aureus typing phage 42D since before 1965. The molecular mechanism of triple conversion mediated by three of these phages was determined by molecular cloning, restriction endonuclease site mapping and hybridization analysis, and compared with the mechanism of beta-lysin and staphylokinase conversion mediated by the serotype F, double-converting phase phi 13. THe genetic determinants mediating expression of enterotoxin A (entA) and staphylokinase (sak) were cloned from the DNA of the triple-converting phage and expression of the cloned determinants detected in Escherichia coli and S. aureus. The entA and sak determinants were closely linked in the phage DNA adjacent to the phage attachment site (attP) in each case and furthermore, the sak determinant of phage phi 13 was also located near its attP. The restriction maps of the entA-, sak- and attP-containing DNA regions of the three triple-converting phages were very similar to each other and to the corresponding sak- and attP- containing DNA region of phage phi 13. Hybridization analysis using a cloned beta-lysin determinant (hlb) and cloned attP-containing DNA fragments as probes demonstrated that beta-lysin conversion mediated by the triple-converting phages and phage phi 13 was caused by insertional inactivation of the chromosomally encoded hlb determinant by orientation-specific integration of phage DNA following lysogenization. FAU - Coleman, D C AU - Coleman DC AD - Department of Microbiology, University of Dublin, Trinity College, Republic of Ireland. FAU - Sullivan, D J AU - Sullivan DJ FAU - Russell, R J AU - Russell RJ FAU - Arbuthnott, J P AU - Arbuthnott JP FAU - Carey, B F AU - Carey BF FAU - Pomeroy, H M AU - Pomeroy HM LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - England TA - J Gen Microbiol JT - Journal of general microbiology JID - 0375371 RN - 0 (Antimicrobial Cationic Peptides) RN - 0 (Bacterial Toxins) RN - 0 (Blood Proteins) RN - 0 (DNA, Recombinant) RN - 0 (DNA, Viral) RN - 0 (Enterotoxins) RN - 0 (Hemolysin Proteins) RN - 0 (Proteins) RN - 0 (Viral Structural Proteins) RN - 0 (beta lysin, human) RN - 37337-57-8 (enterotoxin A, Staphylococcal) RN - EC 3.1.4.12 (Sphingomyelin Phosphodiesterase) RN - EC 3.1.4.12 (hlb protein, Staphylococcus aureus) RN - EC 3.4.24.- (Metalloendopeptidases) RN - EC 3.4.24.29 (auR protein, Staphylococcus aureus) SB - IM MH - *Antimicrobial Cationic Peptides MH - Attachment Sites, Microbiological MH - *Bacterial Toxins MH - Blood Proteins MH - Cross Infection/microbiology MH - DNA, Recombinant MH - DNA, Viral/genetics MH - Enterotoxins/biosynthesis/*genetics MH - Gene Expression Regulation, Bacterial MH - Gene Expression Regulation, Viral MH - Genes, Bacterial MH - Genes, Viral MH - Hemolysin Proteins MH - Humans MH - *Lysogeny MH - Metalloendopeptidases/biosynthesis/*genetics MH - Protein Biosynthesis MH - Proteins/*genetics MH - *Sphingomyelin Phosphodiesterase MH - Staphylococcal Infections/microbiology MH - Staphylococcus Phages/genetics/*isolation & purification/physiology MH - Staphylococcus aureus/*genetics/isolation & purification/pathogenicity MH - Viral Structural Proteins/genetics MH - Virulence EDAT- 1989/06/01 00:00 MHDA- 1989/06/01 00:01 CRDT- 1989/06/01 00:00 PHST- 1989/06/01 00:00 [pubmed] PHST- 1989/06/01 00:01 [medline] PHST- 1989/06/01 00:00 [entrez] AID - 10.1099/00221287-135-6-1679 [doi] PST - ppublish SO - J Gen Microbiol. 1989 Jun;135(6):1679-97. doi: 10.1099/00221287-135-6-1679.