MOLECULAR CHARACTERIZATION AND COMPUTATIONAL STUDIES OF OMPC IN THE CLINICAL ISOLATES OF ESCHERICHIA COLI
Main Article Content
Keywords
OmpC, Computational, In-silico, Antibiotic Resistance
Abstract
Background/aim: Antimicrobial resistance (AMR) is a very severe threat and a major public health issue. Outer Membrane Porin C (OmpC) is an outer membrane protein in bacteria, associated with the modulation of cellular permeability and antibiotic resistance. In this study a clinical strain of Escherichia coli was used to screen for OmpC.
Materials and methods: Genomic DNA of the strain was extracted and screened for the presence of porins by designing specific primers and amplifying the coding gene using conventional PCR. After amplification, PCR product (OmpC gene) was sequenced through Sanger Sequencing method. OmpC of E. coli ATCC and CI were also analyzed by using different computational tools. BLAST and Clustal Omega were used to analyze nucleotide and protein alignment.
Results: Protein alignment result showed various mutations i.e P11S, D47N, V50E, S88N, Q173K, S178D, G233R, L234Y, I235L, T237N, V312I, A358D etc in OmpC amino acid residues of E. coli CI.
Conclusion: Hence, this study determines that the structure as well as the function of OmpC can be altered due to various mutations.
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