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Not AvailableTo combat the action of beta-lactams, Klebsiella pneumoniae launches the enzymatic action by producing beta-lactamases to destruct the activity of ceftazidime and piperacillin. Objective: In our research, we want to know the action of ceftazidime and piperacillin on penicillin-binding protein2 (PBP2) and also does it have any interactions with beta-lactamases (OXA1 and SHV-28). Our idea is to prevent the action of beta-lactamases on ceftazidime and piperacillin. Hence, we have modified the beta-lactam core structures of ceftazidime and piperacillin and done the comparative docking interaction studies. Materials and Methods: K. pneumoniae U25 has been selected for the comparative docking analysis study with ceftazidime and piperacillin antibiotics by modifying its structures and targeting them against PBP2 and beta-lactamases (OXA-1 and SHV-28). Results: Our docking analysis revealed that ceftazidime and modified ceftazidime are forming hydrogen bonds, but piperacillin and modified piperacillin are showing hydrophobic interactions with an active site serine residue (Ser316) of PBP2 responsible for the transpeptidase activity in K. pneumoniae U25. Protective action by beta-lactamases (OXA-1 and SHV-28) to K. pneumoniae U25 against beta-lactam antibiotics is also revealed through our study by docking interactions of Ser71 of OXA-1 and Ser66 of SHV-28 with the ceftazidime, modified ceftazidime, piperacillin, and modified piperacillin.Not Availabl

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Not AvailableIntroduction: Nosocomial infections are a notorious subset of infectious diseases, varying between 10% and 20% prevalence worldwide. The infections are concomitant with various treatment complications, multiple-drug resistance, and a high degree of virulence. Klebsiella pneumoniae is a gram-negative bacteria of nosocomial importance. Objectives: Our current study is gauged to reason and understand why, despite treatment with cutting-edge medicines and technology, the K. pneumoniae remains elusive. Methods: Using various in silico tools, the KPHS_00890 hypothetical protein of K. pneumoniae subsp. pneumoniae HS11286 was identified and annotated. Results: A thorough investigation revealed that KPHS_00890 hypothetical protein is a bifunctional 5′-nucleotidase, an enzyme catalyzing the degradation of nucleotides to nucleosides. Conclusions: Scrutiny and review of the 5′-nucleotidase function across various species ascertained its pertinent role in immune evasion, by suppressing inflammatory responses. Thus, having identified the KPHS_00890 hypothetical protein of K. pneumoniae subsp. pneumoniae HS11286 as a 5′-nucleotidase, we propose that it may be involved in an immune evasion strategy during infection pathogenesis.Not Availabl