Using reverse vaccinology techniques combined with B-cell epitope prediction to screen potential antigenic proteins of the bovine pathogen Clostridium perfringens type A.
Autor: | Qin H; Department of Animal Medicine, Shihezi University, Shihezi, China., Ren J; Department of Animal Medicine, Shihezi University, Shihezi, China., Zeng D; Department of Animal Medicine, Shihezi University, Shihezi, China., Jin R; Department of Animal Medicine, Shihezi University, Shihezi, China., Deng Q; Department of Animal Medicine, Shihezi University, Shihezi, China., Su L; Department of Animal Science, Shihezi University, Shihezi, China., Luo Z; Department of Animal Medicine, Shihezi University, Shihezi, China., Jiang J; Department of Animal Medicine, Shihezi University, Shihezi, China. Electronic address: jiangjianjun@shzu.edu.cn., Wang P; Department of Animal Medicine, Shihezi University, Shihezi, China. Electronic address: wwwpy_322@163.com. |
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Jazyk: | angličtina |
Zdroj: | Microbial pathogenesis [Microb Pathog] 2024 Dec; Vol. 197, pp. 107049. Date of Electronic Publication: 2024 Oct 22. |
DOI: | 10.1016/j.micpath.2024.107049 |
Abstrakt: | Clostridium perfringens type A frequently causes necrohaemorrhagic enteritis in cattle, a rapidly progressing disease with a high mortality rate, thus inflicting substantial economic losses in the cattle industry. Effective prevention and control of this disease rely on rapid detection and vaccination strategies, making the screening of antigenic proteins with diagnostic and vaccine potential particularly crucial. In this study, we conducted a pangenomic analysis of 15 bacterial strains, grounded in traditional reverse vaccinology and supplemented with B-cell linear and conformational epitope analysis tools. This approach led to the identification of 2304 core genes and 3606 accessory genes, among which 58 surface-exposed proteins, encoded by core genes, were identified Proteins lacking tertiary structure information were predicted via AlphaFold2, ultimately identifying four target proteins and 14 candidate proteins enriched with linear and conformational epitopes, including virulence proteins such as alpha-toxin, theta-toxin, and alpha-clostripain, and extracellular solute-binding proteins, rhodanese-like proteins, and the accessory gene-encoded lysozyme inhibitor LprI family protein. Our findings demonstrate that the combined use of multiple B-cell epitope analysis tools can help overcome the limitations of any single tool. The proteins selected in this study offer valuable references for rapid diagnostics and the development of genetically engineered vaccines. Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests:Heqin reports financial support was provided by Supported by the Major Science and Technology Project of the Xinjiang Uygur Autonomous Region, China (Project Name: Key Technologies for Prevention and Control of Common and Multi-Diseases in Cattle, Grant Number: 2023A02007-2). If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (Copyright © 2024 Elsevier Ltd. All rights reserved.) |
Databáze: | MEDLINE |
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