Inhibition of the activity of both domains of lysostaphin through peptidoglycan modification by the lysostaphin immunity protein.
Resistance to lysostaphin, a staphylolytic glycylglycine endopeptidase, is due to a FemABX-like immunity protein that inserts serines in place of some glycines in peptidoglycan cross bridges. These modifications inhibit both binding of the recombinant cell wall targeting domain and catalysis by the recombinant catalytic domain of lysostaphin.
Gargis
Shaw R
SR
Department of Biological Sciences, The University of Alabama, Tuscaloosa, Alabama, USA.
Heath
Harry E
HE
LeBlanc
Paul A
PA
Dekker
Linda
L
Simmonds
Robin S
RS
Sloan
Gary L
GL
D002473:Cell Wall; D008248:Lysostaphin / Q000037:antagonists & inhibitors*; D010457:Peptidoglycan / Q000378:metabolism*; D013210:Staphylococcus / Q000201:enzymology*
D010457:Peptidoglycan; D008248:Lysostaphin