title: Inhibition of the activity of both domains of lysostaphin through peptidoglycan modification by the lysostaphin immunity protein.
abstract: 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.
authors: Department of Biological Sciences, The University of Alabama, Tuscaloosa, Alabama, USA.
authors: Shaw R
authors: SR
authors: Gargis
authors: Harry E
authors: HE
authors: Heath
authors: Paul A
authors: PA
authors: LeBlanc
authors: Linda
authors: L
authors: Dekker
authors: Robin S
authors: RS
authors: Simmonds
authors: Gary L
authors: GL
authors: Sloan
mesh_terms: D002473:Cell Wall; D008248:Lysostaphin / Q000037:antagonists & inhibitors*; D010457:Peptidoglycan / Q000378:metabolism*; D013210:Staphylococcus / Q000201:enzymology*
chemical_list: D010457:Peptidoglycan; D008248:Lysostaphin