Molecular and computational approaches to understand resistance of New Delhi metallo β-lactamase variants (NDM-1, NDM-4, NDM-5, NDM-6, NDM-7)-producing strains against carbapenems

Journal of Biomolecular Structure & Dynamics
Abid AliAsad U Khan

Abstract

The discovery of NDM-1 and its variants has caused the emergence of antibiotic resistance in the community and hospital setting, causing major concern for health care across the globe. New Delhi Metallo-β-lactamase is known to hydrolyse almost all β-lactam antibiotics. Studies have shown the hydrolytic activates of NDM-1 and some of its variants, however a comparative study of these NDM variants has not been explored in detail. Hence, we proposed to check their catalytic activity by performing a comparative study between NDM-1 and its variants. The study was initiated to clone NDM variants (NDM-1, NDM-4, NDM-5, NDM-6 and NDM-7) followed by overexpression of the recombinant proteins to check their hydrolytic properties against β-lactam antibiotics. The minimum inhibitory concentration of carbapenems antibiotics for blaNDM-5 clone was found four fold increased, whereas no change was observed in the clones having other variants. The hydrolytic activity of carbapenem with NDM-5 variant was found to be augmented as per the kinetics parameter where Km was decreased and kcat, kcat/Km values increased as compared to the NDM-1. Molecular docking studies were employed to identify the variations in the binding ability among all NDM varian...Continue Reading

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Feb 20, 2018·International Journal of Biological Macromolecules·Abid AliAsad U Khan

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Citations

May 3, 2019·Journal of Biomolecular Structure & Dynamics·Tristan RichardGrégory Da Costa
Apr 3, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Yilin ZhangKewu Yang
Jan 7, 2021·Future Microbiology·Muhammad Usman QamarMark A Toleman

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Methods Mentioned

BETA
PCR

Software Mentioned

GROMACS
ProModII
Swiss Model
Autodock Vina
mmpbsa
RAMPAGE
AutoDockVina
Autodock
AMBER
Gromos96

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