Cargando…
Mutation and Interaction Analysis of the Glycoprotein D and L and Thymidine Kinase of Pseudorabies Virus
Pseudorabies (also called Aujeszky’s disease) is a highly infectious viral disease caused by the pseudorabies virus (PRV, or Suid herpesvirus 1). Although the disease has been controlled by immunization with the PRV-attenuated vaccine, the emerging PRV variants can escape the immune surveillance in...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9570442/ https://www.ncbi.nlm.nih.gov/pubmed/36232898 http://dx.doi.org/10.3390/ijms231911597 |
_version_ | 1784810107791474688 |
---|---|
author | Li, Xue Chen, Si Zhang, Liying Zheng, Jiawei Niu, Guyu Yang, Lin Zhang, Xinwei Ren, Linzhu |
author_facet | Li, Xue Chen, Si Zhang, Liying Zheng, Jiawei Niu, Guyu Yang, Lin Zhang, Xinwei Ren, Linzhu |
author_sort | Li, Xue |
collection | PubMed |
description | Pseudorabies (also called Aujeszky’s disease) is a highly infectious viral disease caused by the pseudorabies virus (PRV, or Suid herpesvirus 1). Although the disease has been controlled by immunization with the PRV-attenuated vaccine, the emerging PRV variants can escape the immune surveillance in the vaccinated pig, resulting in recent outbreaks. Furthermore, the virus has been detected in other animals and humans, indicating cross-transmission of PRV. However, the mechanism of PRV cross-species transmission needs further study. In this study, we compared the amino acid sequences of glycoproteins (gD), gL, and thymidine kinase (TK) of PRV strains, human PRV hSD-1 2019 strain, and the attenuated strain Bartha-K61, followed by predication of their spatial conformation. In addition, the interactions between the viral gD protein and host nectin-1, nectin-2, and HS were also evaluated via molecular docking. The results showed that the amino acid sequence homology of the gD, gL, and TK proteins of hSD-1 2019 and JL-CC was 97.5%, 94.4%, and 99.1%, respectively. Moreover, there were mutations in the amino acid sequences of gD, gL, and TK proteins of hSD-1 2019 and JL-CC compared with the corresponding reference sequences of the Bartha strain. The mutations of gD, gL, and TK might not affect the spatial conformation of the protein domain but may affect the recognition of antibodies and antigen epitopes. Moreover, the gD protein of JL-CC, isolated previously, can bind to human nectin-1, nectin-2, and HS, suggesting the virus may be highly infectious and pathogenic to human beings. |
format | Online Article Text |
id | pubmed-9570442 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-95704422022-10-17 Mutation and Interaction Analysis of the Glycoprotein D and L and Thymidine Kinase of Pseudorabies Virus Li, Xue Chen, Si Zhang, Liying Zheng, Jiawei Niu, Guyu Yang, Lin Zhang, Xinwei Ren, Linzhu Int J Mol Sci Article Pseudorabies (also called Aujeszky’s disease) is a highly infectious viral disease caused by the pseudorabies virus (PRV, or Suid herpesvirus 1). Although the disease has been controlled by immunization with the PRV-attenuated vaccine, the emerging PRV variants can escape the immune surveillance in the vaccinated pig, resulting in recent outbreaks. Furthermore, the virus has been detected in other animals and humans, indicating cross-transmission of PRV. However, the mechanism of PRV cross-species transmission needs further study. In this study, we compared the amino acid sequences of glycoproteins (gD), gL, and thymidine kinase (TK) of PRV strains, human PRV hSD-1 2019 strain, and the attenuated strain Bartha-K61, followed by predication of their spatial conformation. In addition, the interactions between the viral gD protein and host nectin-1, nectin-2, and HS were also evaluated via molecular docking. The results showed that the amino acid sequence homology of the gD, gL, and TK proteins of hSD-1 2019 and JL-CC was 97.5%, 94.4%, and 99.1%, respectively. Moreover, there were mutations in the amino acid sequences of gD, gL, and TK proteins of hSD-1 2019 and JL-CC compared with the corresponding reference sequences of the Bartha strain. The mutations of gD, gL, and TK might not affect the spatial conformation of the protein domain but may affect the recognition of antibodies and antigen epitopes. Moreover, the gD protein of JL-CC, isolated previously, can bind to human nectin-1, nectin-2, and HS, suggesting the virus may be highly infectious and pathogenic to human beings. MDPI 2022-09-30 /pmc/articles/PMC9570442/ /pubmed/36232898 http://dx.doi.org/10.3390/ijms231911597 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Li, Xue Chen, Si Zhang, Liying Zheng, Jiawei Niu, Guyu Yang, Lin Zhang, Xinwei Ren, Linzhu Mutation and Interaction Analysis of the Glycoprotein D and L and Thymidine Kinase of Pseudorabies Virus |
title | Mutation and Interaction Analysis of the Glycoprotein D and L and Thymidine Kinase of Pseudorabies Virus |
title_full | Mutation and Interaction Analysis of the Glycoprotein D and L and Thymidine Kinase of Pseudorabies Virus |
title_fullStr | Mutation and Interaction Analysis of the Glycoprotein D and L and Thymidine Kinase of Pseudorabies Virus |
title_full_unstemmed | Mutation and Interaction Analysis of the Glycoprotein D and L and Thymidine Kinase of Pseudorabies Virus |
title_short | Mutation and Interaction Analysis of the Glycoprotein D and L and Thymidine Kinase of Pseudorabies Virus |
title_sort | mutation and interaction analysis of the glycoprotein d and l and thymidine kinase of pseudorabies virus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9570442/ https://www.ncbi.nlm.nih.gov/pubmed/36232898 http://dx.doi.org/10.3390/ijms231911597 |
work_keys_str_mv | AT lixue mutationandinteractionanalysisoftheglycoproteindandlandthymidinekinaseofpseudorabiesvirus AT chensi mutationandinteractionanalysisoftheglycoproteindandlandthymidinekinaseofpseudorabiesvirus AT zhangliying mutationandinteractionanalysisoftheglycoproteindandlandthymidinekinaseofpseudorabiesvirus AT zhengjiawei mutationandinteractionanalysisoftheglycoproteindandlandthymidinekinaseofpseudorabiesvirus AT niuguyu mutationandinteractionanalysisoftheglycoproteindandlandthymidinekinaseofpseudorabiesvirus AT yanglin mutationandinteractionanalysisoftheglycoproteindandlandthymidinekinaseofpseudorabiesvirus AT zhangxinwei mutationandinteractionanalysisoftheglycoproteindandlandthymidinekinaseofpseudorabiesvirus AT renlinzhu mutationandinteractionanalysisoftheglycoproteindandlandthymidinekinaseofpseudorabiesvirus |