Omp 36 mediated meropenem resistance in clinical isolates of klebsiella pneumonia

β-lactamase genes have evolved over the years with improved specificity and an extended array of antibiotic profile. The impact on resistance is also attributed to the intrinsic mechanisms of porin channel mediated transport of antibiotics. We here reported the intrinsic mechanism of porin channel mediated transport in meropenem resistant clinical isolates of Klebsiella pneumoniae. A total of 52 meropenem resistant K. pneumoniae isolates were selected and the antibiotic resistant gene status of TEM, CTX-M, SHV, NDM and OXA-48 and the omp 35 and 36 were detected through PCR. These isolates were selected on the basis of their phenotypic expression of β-lactamase production tested as per the Clinical & Laboratories Standards Institute (CLSI) guidelines, 2011. Four isolates based on the presence of the resistant genes were then selected as representatives to study the omp36 porin channel. Sequence analysis of all the representatives of omp36 from Kp08, Kp12, Kp13 and Kp36 plausibly suggested the presence of significant mutation. Structure analysis of all the representatives by in silico modelling, structure refinement and energy minimization showed that Kp12 has the abnormal organization of β-barrel omp36 porin channel where an extended β-sheet was blocking the channel core. Molecular docking analysis deciphered the blocking of meropenem antibiotics through the channel pore hindered by the mutant omp36. Variations in the gene sequence of omp36 have shown to affect meropenem resistance in K. pneumoniae which is observed to be just as sinister for treatment in clinical setting.