Identification of Linear Epitopes in the C-Terminal Region of ASFV p72 Protein
African swine fever, which is induced by the African swine fever virus (ASFV), poses a significant threat to the global pig industry due to its high lethality in domestic pigs and wild boars. Despite the severity of the disease, there is a lack of effective vaccines and drugs against the ASFV. The p...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-11-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/11/12/2846 |
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| author | Yifan Hu Anchen Wang Wanwan Yan Junbo Li Xin Meng Lingchao Chen Songnan Li Wu Tong Ning Kong Lingxue Yu Hai Yu Tongling Shan Jiaping Xu Guangzhi Tong Hao Zheng |
| author_facet | Yifan Hu Anchen Wang Wanwan Yan Junbo Li Xin Meng Lingchao Chen Songnan Li Wu Tong Ning Kong Lingxue Yu Hai Yu Tongling Shan Jiaping Xu Guangzhi Tong Hao Zheng |
| author_sort | Yifan Hu |
| collection | DOAJ |
| description | African swine fever, which is induced by the African swine fever virus (ASFV), poses a significant threat to the global pig industry due to its high lethality in domestic pigs and wild boars. Despite the severity of the disease, there is a lack of effective vaccines and drugs against the ASFV. The p72 protein, constituting 31 to 33% of the total virus particle mass, serves as the primary capsid protein of ASFV. It is a crucial antigen for the development of ASF subunit vaccines and serological diagnostic methods. In this investigation, 27 monoclonal antibodies (mAbs) were generated through mouse immunization with the truncated C-terminal p72 protein expressed by <i>Escherichia coli.</i> Among these, six mAbs exhibited binding to the p72 trimer, with their respective recognized epitopes identified as <sup>542</sup>VTAHGINLIDKF<sup>553</sup>, <sup>568</sup>GNAIKTP<sup>574</sup>, and <sup>584</sup>FALKPREEY<sup>592</sup>. All three epitopes were situated within the interval sequences of functional units of the C-terminal jelly-roll barrel of p72. Notably, two epitopes, <sup>568</sup>GNAIKTP<sup>574</sup> and <sup>584</sup>FALKPREEY<sup>592</sup>, were internal to the p72 trimer, while the epitope <sup>542</sup>VTAHGINLIDKF<sup>553</sup> was exposed on the surface of the trimer and consistently conserved across all ASFV genotypes. These findings enhance our comprehension of the antigenic function and structure of the p72 protein, facilitating the utilization of p72 in the development of diagnostic techniques for ASFV. |
| first_indexed | 2024-03-08T20:31:41Z |
| format | Article |
| id | doaj.art-287ef337137840e6aabf1d887c8f06d8 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-08T20:31:41Z |
| publishDate | 2023-11-01 |
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| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-287ef337137840e6aabf1d887c8f06d82023-12-22T14:25:42ZengMDPI AGMicroorganisms2076-26072023-11-011112284610.3390/microorganisms11122846Identification of Linear Epitopes in the C-Terminal Region of ASFV p72 ProteinYifan Hu0Anchen Wang1Wanwan Yan2Junbo Li3Xin Meng4Lingchao Chen5Songnan Li6Wu Tong7Ning Kong8Lingxue Yu9Hai Yu10Tongling Shan11Jiaping Xu12Guangzhi Tong13Hao Zheng14Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaCollege of Life Sciences, Anhui Agricultural University, Hefei 230031, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, ChinaAfrican swine fever, which is induced by the African swine fever virus (ASFV), poses a significant threat to the global pig industry due to its high lethality in domestic pigs and wild boars. Despite the severity of the disease, there is a lack of effective vaccines and drugs against the ASFV. The p72 protein, constituting 31 to 33% of the total virus particle mass, serves as the primary capsid protein of ASFV. It is a crucial antigen for the development of ASF subunit vaccines and serological diagnostic methods. In this investigation, 27 monoclonal antibodies (mAbs) were generated through mouse immunization with the truncated C-terminal p72 protein expressed by <i>Escherichia coli.</i> Among these, six mAbs exhibited binding to the p72 trimer, with their respective recognized epitopes identified as <sup>542</sup>VTAHGINLIDKF<sup>553</sup>, <sup>568</sup>GNAIKTP<sup>574</sup>, and <sup>584</sup>FALKPREEY<sup>592</sup>. All three epitopes were situated within the interval sequences of functional units of the C-terminal jelly-roll barrel of p72. Notably, two epitopes, <sup>568</sup>GNAIKTP<sup>574</sup> and <sup>584</sup>FALKPREEY<sup>592</sup>, were internal to the p72 trimer, while the epitope <sup>542</sup>VTAHGINLIDKF<sup>553</sup> was exposed on the surface of the trimer and consistently conserved across all ASFV genotypes. These findings enhance our comprehension of the antigenic function and structure of the p72 protein, facilitating the utilization of p72 in the development of diagnostic techniques for ASFV.https://www.mdpi.com/2076-2607/11/12/2846African swine fever virusp72 proteinmonoclonal antibodyepitope |
| spellingShingle | Yifan Hu Anchen Wang Wanwan Yan Junbo Li Xin Meng Lingchao Chen Songnan Li Wu Tong Ning Kong Lingxue Yu Hai Yu Tongling Shan Jiaping Xu Guangzhi Tong Hao Zheng Identification of Linear Epitopes in the C-Terminal Region of ASFV p72 Protein Microorganisms African swine fever virus p72 protein monoclonal antibody epitope |
| title | Identification of Linear Epitopes in the C-Terminal Region of ASFV p72 Protein |
| title_full | Identification of Linear Epitopes in the C-Terminal Region of ASFV p72 Protein |
| title_fullStr | Identification of Linear Epitopes in the C-Terminal Region of ASFV p72 Protein |
| title_full_unstemmed | Identification of Linear Epitopes in the C-Terminal Region of ASFV p72 Protein |
| title_short | Identification of Linear Epitopes in the C-Terminal Region of ASFV p72 Protein |
| title_sort | identification of linear epitopes in the c terminal region of asfv p72 protein |
| topic | African swine fever virus p72 protein monoclonal antibody epitope |
| url | https://www.mdpi.com/2076-2607/11/12/2846 |
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