Expression of the genes for lysostaphin and lysostaphin resistance in streptococci

Abstract

To determine if the genes for lysostaphin endopeptidase (end) and lysostaphin resistance (epr) function in streptococci, we transferred these genes from Staphylococcus simulans biovar staphylolyticus into two strains of Streptococcus equi subsp. zooepidemicus. The endcontaining streptococci were able to produce and process proendopeptidase. Strains containing epr were more resistant to lysis by the streptococcolytic enzyme zoocin A and amino acid analysis of the peptidoglycans of the epr-containing streptococci revealed insertion of serines in their cross bridges. This is the first report of the transfer of a femABX-like immunity factor resulting in a physiologically useful effect in a different genus.

Characterization of a novel family of fibronectin‐binding proteins with M23 peptidase domains from Treponema denticola

“…, 1998) are enzymic and replace peptidoglycan glycines with serines (DeHart et al. , 1995; Heath Farris et al. , 2003), which prevents successful targeting of the substrate‐binding domain and inhibiting hydrolysis (Lai et al.…”