Publications

cloning and expression in escherichia coli and staphylococcus aureus of the beta-lysin determinant from staphylococcus aureus: evidence that bacteriophage conversion of beta-lysin activity is caused by insertional inactivation of the beta-lysin determinant.	the beta-lysin determinant (hlb) from staphylococcus aureus cn6708 was cloned in escherichia coli k-12 using the bacteriophage replacement vector lambda l47.1. the hlb determinant was localised to a 1250 base pair dna sequence by cloning fragments from a hlb+ recombinant phage into the plasmid vectors pacyc184 and pbr322 in e. coli k-12, and by the subsequent construction and analysis of several sub-clones, in vitro deletion and tn5 insertion mutations. e. coli cells harbouring hlb+ plasmids exp ...	1986	3334158
staphylococcus aureus bacteriophages mediating the simultaneous lysogenic conversion of beta-lysin, staphylokinase and enterotoxin a: molecular mechanism of triple conversion.	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 ...	1989	2533245
insertional inactivation of the staphylococcus aureus beta-toxin by bacteriophage phi 13 occurs by site- and orientation-specific integration of the phi 13 genome.	lysogenization of staphylococcus aureus by the serotype f converting bacteriophage phi 13 results in loss of beta-toxin expression. sequence analysis of the s. aureus beta-toxin gene (hlb), the attachment site (attp)-containing region of phi 13 dna and the chromosome/bacteriophage dna junctions of a phi 13 lysogen, revealed that the molecular mechanism of loss of beta-toxin expression was due to insertion of the phi 13 genome into the 5' end of hlb. the insertion site (attb) within hlb contained ...	1991	1830359
serotype f double- and triple-converting phage insertionally inactivate the staphylococcus aureus beta-toxin determinant by a common molecular mechanism.	the precise molecular mechanism of staphylococcus aureus beta-toxin inactivation by the serotype f triple-converting phage phi 42, phi a1 and phi a3 was investigated. sequence analysis of the phi 42 (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 tha ...	1993	8454180
characterization of phi 13, a bacteriophage related to phi 6 and containing three dsrna genomic segments.	the three dsrna genomic segments of bacteriophage phi 13 were copied as cdna and the nucleotide sequences were determined. the organization of the genome is similar to that of phi 6, and there is significant similarity in the amino acid sequences of the proteins of the polymerase complex and one of the membrane proteins, p6. there is little or no similarity in the nucleotide sequences. several features of the viral proteins differ markedly from those of phi 6. although both phages are covered by ...	2000	11017801