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Structure of the catalytic domain of the colistin resistance enzyme MCR-1

Stojanoski, Vlatko ; Sankaran, Banumathi ; Prasad, B. V. Venkataram ; Poirel, Laurent ; Nordmann, Patrice ; Palzkill, Timothy

In: BMC Biology, 2016, vol. 14, p. 81

Due to the paucity of novel antibiotics, colistin has become a last resort antibiotic for treating multidrug resistant bacteria. Colistin acts by binding the lipid A component of lipopolysaccharides and subsequently disrupting the bacterial membrane. The recently identified plasmid-encoded MCR-1 enzyme is the first transmissible colistin resistance determinant and is a cause for concern for...

Comment on: Resistance gene naming and numbering: is it a new gene or not?

Jacoby, George A. ; Bonomo, Robert A. ; Bradford, Patricia A. ; Bush, Karen ; Doi, Yohei ; Feldgarden, Michael ; Haft, Daniel ; Klimke, William ; Nordmann, Patrice ; Palzkill, Timothy ; Poirel, Laurent ; Prasad, Arjun ; Rossolini, Gian Maria ; Walsh, Timothy

In: Journal of Antimicrobial Chemotherapy, 2016, p. dkw204

Structural basis for different substrate profiles of two closely related class D β-lactamases and their inhibition by halogens

Stojanoski, Vlatko ; Chow, Dar-Chone ; Fryszczyn, Bartlomiej ; Hu, Liya ; Nordmann, Patrice ; Poirel, Laurent ; Sankaran, Banumathi ; Prasad, B. V. Venkataram ; Palzkill, Timothy

In: Biochemistry, 2015, vol. 54, no. 21, p. 3370–3380

OXA-163 and OXA-48 are closely related class D β-lactamases that exhibit different substrate profiles. OXA-163 hydrolyzes oxyimino-cephalosporins, particularly ceftazidime, while OXA-48 prefers carbapenem substrates. OXA-163 differs from OXA-48 by one substitution (S212D) in the active-site β5 strand and a four-amino acid deletion (214-RIEP-217) in the loop connecting the β5 and β6 strands....