Food and Fermentation Industries >

2024 , Vol. 50 >Issue 12: 251 - 257

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.037068

Bioinformatics analysis and molecular dynamics simulation of thermolabile hemolysin in Vibrio parahaemolyticus

  • ZHANG Defu ,
  • YU Zhenxing ,
  • ZHANG Ming ,
  • LYU Xinran ,
  • ZHANG Yongqin ,
  • ZHANG Guoqing ,
  • LI Jianrong
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  • 1(College of Food Science and Engineering, Institute of Ocean, Bohai University, National and Local Joint Engineering Research Center for Storage, Processing and Safety Control Technology of Fresh Agricultural Products, Jinzhou 121013, China)
    2(Shandong Meijia Group Co., Ltd., Rizhao 276806, China)
    3(Jinzhou Agricultural and Rural Comprehensive Service Center Aquatic Technology Extension Station, Jinzhou 121013, China)

Received date: 2023-08-15

  Revised date: 2023-08-28

  Online published: 2024-07-11

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Abstract

Vibrio parahaemolyticus is a Gram-negative zoonotic pathogen, which can cause food-borne diseases such as human gastroenteritis.V.parahaemolyticus has many virulence factors and thermolabile hemolysin (TLH) is one of them.In this study, the tlh gene of V.parahaemolyticus was cloned and sequenced, and the bioinformatics analysis and structural and functional prediction of TLH protein were carried out. Results showed that the TLH consisted of 418 amino acids with a predicted molecular weight of 47.36 kDa.Several conserved domains and motifs were identified in TLH protein, including SGNH hydrolase domain and GDSL motif.Based on the homologous modeling and verification of the three-dimensional structure of TLH protein, the stability of TLH protein, the interaction ability with 4-nitrophenyl laurate and the influence of binding substrate on the structure compactness and residue flexibility were analyzed by molecular dynamics simulation.It was revealed that the periphery of the catalytic triad Ser153-His390-Asp393 is an important drug target active pocket with highly conserved residue sequences, and the residues showed flexibility difference after substrate binding.This study analyzed the properties and structure of V.parahaemolyticus TLH, which can provide theoretical support for ensuring the safety of aquatic products and improving the safety evaluation level of aquatic raw materials.

Key words： gene cloning; Vibrio parahaemolyticus; thermolabile hemolysin (tlh); bioinformatics analysis; molecular dynamics simulation

Cite this article

ZHANG Defu , YU Zhenxing , ZHANG Ming , LYU Xinran , ZHANG Yongqin , ZHANG Guoqing , LI Jianrong . Bioinformatics analysis and molecular dynamics simulation of thermolabile hemolysin in Vibrio parahaemolyticus[J]. Food and Fermentation Industries, 2024 , 50(12) : 251 -257 . DOI: 10.13995/j.cnki.11-1802/ts.037068

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