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The emergence of β-lactam resistance is yearning for clinical significance in  Enterobacteriaceae , which are categorized under global priority pathogen lists by the World Health Organization. Likewise, the prevalence of numerous β-lactamase enzymes, mutational propensity in such bacteria, and their role in accelerating resistance is still a major concern. Thus, the present work intends to characterize the β-lactamase producing bacteria isolated from acute diarrheal patients to understand their chromosomally acquired resistance pattern through molecular characterization and  in silico  approaches. The current study highlights the first identified  Escherichia fergusonii  and  Escherichia marmotae  species and their β-lactamase encoding genes,  bla OKP-A,  bla NDM and  bla OXA from the unexplored  Enterobacteriaceae  family from North East India. First-ever reported point mutations such as Arg32Ser, His92Tyr, and Leu147Phe were observed in BlaSHV protein of two  Klebsiella pneumoniae  isolates S-35 and S-46. In molecular docking, non-catalytic site H-bond interactions of Arg 218, Ala 223, Asn 128, Ser 126, Gln 95, Asp 100, Tyr 101, Ser 102, Ala 274 with a low binding affinity towards BlaSHV was found. This correlates with the high imipenem, ceftazidime, cefuroxime, ceftriaxone, and cefpodoxime resistance in  Klebsiella pneumoniae  S-35 with the complementary effect of mutations Arg32Ser and Leu147Phe. Besides, the role of His92Tyr mutation in controlling the resistance in  Klebsiella pneumoniae  S-46 is also illustrated. Thus, our study highlights the novel mutations of β-lactamase and its clinical importance with altered resistance profiles. This could be useful to design better therapeutics and to readjust antibiotic treatment regimes against them and control to grow more resistance under selective pressure. Communicated by Ramaswamy H. Sarma

journal of biomolecular structure and dynamics

Identification of Arg32Ser, His92Tyr and Leu147Phe novel mutations in chromosomally mediated β-lactamase SHV and  in silico  characterization to understand their substrate activity imparting resistance