4.5 Article

In silico screening and validation of KPHS_00890 protein of Klebsiella pneumoniae proteome: An application to bacterial resistance and pathogenesis

Journal

JOURNAL OF KING SAUD UNIVERSITY SCIENCE
Volume 33, Issue 6, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.jksus.2021.101537

Keywords

Molecular docking; Homology modeling; Phylogenetic tree; 5 '-nucleotidase; Klebsiella pneumoniae; Multiple sequence alignment

Funding

  1. JSS Academy of Higher Education and Research (JSSAHER), Mysuru, India
  2. King Saud University, Riyadh, Saudi Arabia [RSP-2021/56]

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Nosocomial infections, including those caused by Klebsiella pneumoniae, are highly virulent and often resistant to multiple drugs. The KPHS_00890 hypothetical protein of K. pneumoniae has been identified as a bifunctional 5'-nucleotidase, with a potential role in immune evasion strategies during infection.
Introduction: 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. (C) 2021 The Authors. Published by Elsevier B.V. on behalf of King Saud University.

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