Identification of a Conserved Linear Epitope on the p54 Protein of African Swine Fever Virus

African swine fever virus (ASFV) is a highly virulent pathogen that causes nearly 100% mortality in acute infections and poses persistent risks. Effective containment of ASFV outbreaks requires rapid and reliable diagnostic tools. The p54 protein, a key structural component of ASFV, has emerged as a...

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Main Authors: Kuijing He, Yue Wu, Zhipeng Su, Yue Zeng, Guishan Ye, Qi Wu, Long Li, Anding Zhang
Format: Article
Language:English
Published: MDPI AG 2025-06-01
Series:Viruses
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Online Access:https://www.mdpi.com/1999-4915/17/6/823
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author Kuijing He
Yue Wu
Zhipeng Su
Yue Zeng
Guishan Ye
Qi Wu
Long Li
Anding Zhang
author_facet Kuijing He
Yue Wu
Zhipeng Su
Yue Zeng
Guishan Ye
Qi Wu
Long Li
Anding Zhang
author_sort Kuijing He
collection DOAJ
description African swine fever virus (ASFV) is a highly virulent pathogen that causes nearly 100% mortality in acute infections and poses persistent risks. Effective containment of ASFV outbreaks requires rapid and reliable diagnostic tools. The p54 protein, a key structural component of ASFV, has emerged as an important target for serological detection. Herein, the recombinant p54 protein (amino acids 53–184) was expressed in <i>Escherichia coli</i>, and three mouse monoclonal antibodies (mAbs) (IgG1/kappa subtype) were developed. Among these mAbs, the mAb 1F9 specifically recognized the B-cell epitope <sup>66</sup>IQFINPYQDQQ<sup>76</sup>, which is conserved across different genotypes of ASFV, suggesting that the epitope may serve as a valuable target for serological detection of ASFV. Structural modeling analysis revealed that this epitope is surface-exposed on the p54 protein, with <sup>67</sup>Gln and <sup>68</sup>Phe identified as critical residues for 1F9 binding. Moreover, a blocking ELISA based on the mAb 1F9 was established for detecting ASFV-specific antibodies in clinical serum samples, achieving a coincidence rate exceeding 95%. These findings demonstrate that mAb 1F9, targeting a conserved and accessible region of p54, represents a valuable tool for ASFV serodiagnosis, surveillance, and outbreak management.
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spelling doaj-art-ba7fd318691441dcbd9522d0431e877e2025-08-20T03:29:52ZengMDPI AGViruses1999-49152025-06-0117682310.3390/v17060823Identification of a Conserved Linear Epitope on the p54 Protein of African Swine Fever VirusKuijing He0Yue Wu1Zhipeng Su2Yue Zeng3Guishan Ye4Qi Wu5Long Li6Anding Zhang7State Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, ChinaState Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, ChinaDekon Food and Agriculture Group, Chengdu 610200, ChinaState Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, ChinaState Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, ChinaState Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, ChinaState Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, ChinaState Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, ChinaAfrican swine fever virus (ASFV) is a highly virulent pathogen that causes nearly 100% mortality in acute infections and poses persistent risks. Effective containment of ASFV outbreaks requires rapid and reliable diagnostic tools. The p54 protein, a key structural component of ASFV, has emerged as an important target for serological detection. Herein, the recombinant p54 protein (amino acids 53–184) was expressed in <i>Escherichia coli</i>, and three mouse monoclonal antibodies (mAbs) (IgG1/kappa subtype) were developed. Among these mAbs, the mAb 1F9 specifically recognized the B-cell epitope <sup>66</sup>IQFINPYQDQQ<sup>76</sup>, which is conserved across different genotypes of ASFV, suggesting that the epitope may serve as a valuable target for serological detection of ASFV. Structural modeling analysis revealed that this epitope is surface-exposed on the p54 protein, with <sup>67</sup>Gln and <sup>68</sup>Phe identified as critical residues for 1F9 binding. Moreover, a blocking ELISA based on the mAb 1F9 was established for detecting ASFV-specific antibodies in clinical serum samples, achieving a coincidence rate exceeding 95%. These findings demonstrate that mAb 1F9, targeting a conserved and accessible region of p54, represents a valuable tool for ASFV serodiagnosis, surveillance, and outbreak management.https://www.mdpi.com/1999-4915/17/6/823monoclonal antibodyAfrican swine fever virusp54 proteinB-cell epitopeblocking ELISA
spellingShingle Kuijing He
Yue Wu
Zhipeng Su
Yue Zeng
Guishan Ye
Qi Wu
Long Li
Anding Zhang
Identification of a Conserved Linear Epitope on the p54 Protein of African Swine Fever Virus
Viruses
monoclonal antibody
African swine fever virus
p54 protein
B-cell epitope
blocking ELISA
title Identification of a Conserved Linear Epitope on the p54 Protein of African Swine Fever Virus
title_full Identification of a Conserved Linear Epitope on the p54 Protein of African Swine Fever Virus
title_fullStr Identification of a Conserved Linear Epitope on the p54 Protein of African Swine Fever Virus
title_full_unstemmed Identification of a Conserved Linear Epitope on the p54 Protein of African Swine Fever Virus
title_short Identification of a Conserved Linear Epitope on the p54 Protein of African Swine Fever Virus
title_sort identification of a conserved linear epitope on the p54 protein of african swine fever virus
topic monoclonal antibody
African swine fever virus
p54 protein
B-cell epitope
blocking ELISA
url https://www.mdpi.com/1999-4915/17/6/823
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