Anindya Sundar Ghosh

Rv0783c of Mycobacterium tuberculosis acts as a proton-motive force dependent multidrug efflux transporter involved in the efflux of structurally unrelated antibiotics and enhancing biofilm formation

This study identifies Rv0783c as a multidrug efflux transporter in Mycobacterium tuberculosis that enhances antibiotic resistance and biofilm formation.

Placentrex disrupts the biofilm formation of Pseudomonas aeruginosa through multi-target transcriptional reprogramming.

This paper evaluates Placentrex's antibacterial and antibiofilm activity against Pseudomonas aeruginosa, identifying its mechanism involving multi-target transcriptional reprogramming.

Deciphering the role of the non-active site ancillary residues in maintaining the activity and substrate specificity of OXA-232 beta-lactamase

This study investigates the role of non-active site residues in OXA-232 beta-lactamase, showing their impact on activity, substrate specificity, and structural stability through site-directed mutagenesis and biophysical analysis.

Deletion of major shell proteins of ethanolamine utilization microcompartment reduces intrinsic antibiotic resistance, biofilm, and intracellular survival of Salmonella Typhimurium

Putative MFS transporter Rv1250 of Mycobacterium tuberculosis is involved in multidrug efflux activity

This study identifies Rv1250 as a multidrug efflux pump in Mycobacterium tuberculosis that enhances drug resistance by facilitating drug extrusion and biofilm formation.

Conserved ancillary residues situated proximally to the VIM-2 active site affect its metallo β-lactamase activity

The paper investigates the impact of specific amino acid substitutions near the VIM-2 active site on its metallo β-lactamase activity and stability, finding that N210A and D182A reduce catalytic efficiency and thermal stability.

A magnesium transporter CorA of Mycobacterium smegmatis enhances the tolerance of structurally unrelated antibiotics in the host cells

This study shows that the magnesium transporter CorA in Mycobacterium smegmatis and E. coli increases tolerance to structurally unrelated antibiotics and enhances biofilm formation.

Acinetobacter baumannii DacC influences cell shape, biofilm formation, and physiological fitness by manifesting DD-carboxypeptidase and β-lactamase dual-enzyme activities

This study identifies DacC in Acinetobacter baumannii as a dual-enzyme with DD-carboxypeptidase and β-lactamase activities that affect cell shape, biofilm formation, and antibiotic susceptibility.