Rkr. Voladri et Ds. Kernodle, Characterization of a chromosomal gene encoding type B beta-lactamase in phage group II isolates of Staphylococcus aureus, ANTIM AG CH, 42(12), 1998, pp. 3163-3168
In contrast to most Staphylococcus aureus isolates in which the gene for st
aphylococcal beta-lactamase (blaZ) is plasmid borne, isolates typeable by g
roup II bacteriophages frequently carry blaZ on the chromosome. Furthermore
, the chromosomal gene encodes the type B variant of staphylococcal beta-la
ctamase for which the nucleotide and deduced amino acid sequences have not
yet been reported. To better understand beta-lactamase production among pha
ge group II staphylococci and the nature of the type B beta-lactamase, we d
etermined the type and amount of enzyme produced by 24 phage group II isola
tes. Of these isolates, 1 did not produce beta-lactamase, 8 produced the ty
pe B enzyme, and 15 produced the type C enzyme. In all eight type B beta-la
ctamase-producing isolates, blaZ was located on the chromosome. This was in
contrast to the type C beta-lactamase-producing isolates, in which blaZ wa
s located on a 21-kb plasmid. The nucleotide sequence corresponding to the
leader peptide and the N-terminal 85% of the mature exoenzyme form of type
B S. aureus was determined. The deduced amino acid sequence revealed 3 resi
dues in the leader peptide and 12 residues in the exoenzyme portion of the
beta-lactamase that differ from the prototypic type A beta-lactamase sequen
ce. These include the serine-to-asparagine change at residue 216 found in t
he kinetically similar type C enzyme, a threonine-to-lysine change at resid
ue 128 close to the SDN loop (residues 130 to 132), and several substitutio
ns not found in any of the other staphylococcal beta-lactamases. In summary
modern isolates of S. aureus typeable by group II phages produce type B or
type C staphylococcal beta-lactamase. The type B gene resides on the chrom
osome and has a sequence that, when compared to the sequences of the other
staphylococcal beta-lactamases, corresponds well with its kinetic propertie
s.