Genomics & Informatics

Korea Genome Organization (한국유전체학회)
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In silico annotation of a hypothetical protein from Listeria monocytogenes EGD-e unfolds a toxin protein of the type II secretion system

  • Maisha Tasneem (Department of Biotechnology and Genetic Engineering, Noakhali Science and Technology University) ;
  • Shipan Das Gupta (Department of Biotechnology and Genetic Engineering, Noakhali Science and Technology University) ;
  • Monira Binte Momin (Department of Biotechnology and Genetic Engineering, Noakhali Science and Technology University) ;
  • Kazi Modasser Hossain (Department of Biotechnology and Genetic Engineering, Noakhali Science and Technology University) ;
  • Tasnim Binta Osman (Department of Biotechnology and Genetic Engineering, Noakhali Science and Technology University) ;
  • Fazley Rabbi (Department of Biotechnology and Genetic Engineering, Noakhali Science and Technology University)
  • Received : 2022.11.09
  • Accepted : 2023.01.03
  • Published : 2023.03.31
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Abstract

The gram-positive bacterium Listeria monocytogenes is an important foodborne intracellular pathogen that is widespread in the environment. The functions of hypothetical proteins (HP) from various pathogenic bacteria have been successfully annotated using a variety of bioinformatics strategies. In this study, a HP Imo0888 (NP_464414.1) from the Listeria monocytogenes EGD-e strain was annotated using several bioinformatics tools. Various techniques, including CELLO, PSORTb, and SOSUIGramN, identified the candidate protein as cytoplasmic. Domain and motif analysis revealed that the target protein is a PemK/MazF-like toxin protein of the type II toxin-antitoxin system (TAS) which was consistent with BLASTp analysis. Through secondary structure analysis, we found the random coil to be the most frequent. The Alpha Fold 2 Protein Structure Prediction Database was used to determine the three-dimensional (3D) structure of the HP using the template structure of a type II TAS PemK/MazF family toxin protein (DB ID_AFDB: A0A4B9HQB9) with 99.1% sequence identity. Various quality evaluation tools, such as PROCHECK, ERRAT, Verify 3D, and QMEAN were used to validate the 3D structure. Following the YASARA energy minimization method, the target protein's 3D structure became more stable. The active site of the developed 3D structure was determined by the CASTp server. Most pathogens that harbor TAS create a crucial risk to human health. Our aim to annotate the HP Imo088 found in Listeria could offer a chance to understand bacterial pathogenicity and identify a number of potential targets for drug development.

Keywords

Acknowledgement

The authors acknowledge the Department of Biotechnology and Genetic Engineering, Noakhali Science and Technology University for providing support to conduct the research work.

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