Inhibition of the Activity of Both Domains of Lysostaphin Through Peptidoglycan Modification by the Lysostaphin Immunity Protein
Overview
Microbiology
Affiliations
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.
Konstantinova S, Grishin A, Lyashchuk A, Vasina I, Karyagina A, Lunin V Appl Microbiol Biotechnol. 2022; 106(19-20):6519-6534.
PMID: 36112205 DOI: 10.1007/s00253-022-12173-w.
Current Knowledge of the Mode of Action and Immunity Mechanisms of LAB-Bacteriocins.
Perez-Ramos A, Madi-Moussa D, Coucheney F, Drider D Microorganisms. 2021; 9(10).
PMID: 34683428 PMC: 8538875. DOI: 10.3390/microorganisms9102107.
Malecki P, Mitkowski P, Jagielska E, Trochimiak K, Mesnage S, Sabala I Int J Mol Sci. 2021; 22(13).
PMID: 34281200 PMC: 8269130. DOI: 10.3390/ijms22137136.
Kang S, Jun J, Moon J, Hong K AMB Express. 2020; 10(1):139.
PMID: 32770428 PMC: 7415045. DOI: 10.1186/s13568-020-01073-9.
Structural bases of peptidoglycan recognition by lysostaphin SH3b domain.
Mitkowski P, Jagielska E, Nowak E, Bujnicki J, Stefaniak F, Niedzialek D Sci Rep. 2019; 9(1):5965.
PMID: 30979923 PMC: 6461655. DOI: 10.1038/s41598-019-42435-z.