Zhengguo Wang , Linlin Mu , Guishan Ye , Kuijing He , Cong Cai , Peiyao Shi , Jieyu Zhou , Yaqin Gan , Yue Zeng , Anding Zhang , Long Li , Li Han
{"title":"一种识别CDV-H蛋白保守表位的中和性单克隆抗体及其胶体金试纸条的研制","authors":"Zhengguo Wang , Linlin Mu , Guishan Ye , Kuijing He , Cong Cai , Peiyao Shi , Jieyu Zhou , Yaqin Gan , Yue Zeng , Anding Zhang , Long Li , Li Han","doi":"10.1016/j.ijbiomac.2025.144800","DOIUrl":null,"url":null,"abstract":"<div><div>Canine distemper virus (CDV) is currently a significant viral disease that poses a threat to the health of pets and the breeding of fur-bearing animals. It is crucial to develop a diagnostic method that can be performed on-site, is simple to execute, and yields intuitively visible results. In this study, a neutralizing monoclonal antibody(mAb) 5-8H targeting the CDV-H protein was developed and characterized. The mAb 5-8H specifically recognizes prevalent CDV strains. The minimal linear epitopes recognized by 5-8H were identified as epitopes 498-607aa, with key amino acids being 531D, 552R, 554T, and 599R. These four key antigenic sites exhibited a high degree of conservation among all CDV strains, with conservatism ranging from 94.39 % to 99.78 %. The three-dimensional structural revealed that the antigenic epitope was exposed on the surface of the CDV-H protein, making it accessible for binding with antibody. Based on mAb 5-8H, a highly sensitive and specific colloidal gold test strip for detecting CDV was developed. This method achieves a concordance rate of 96 % with RT-qPCR and is suitable for rapid detection of CDV.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"316 ","pages":"Article 144800"},"PeriodicalIF":8.5000,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Development of a neutralizing monoclonal antibody recognizing a conserved epitope of CDV-H protein and its colloidal gold test strip for antigen detection\",\"authors\":\"Zhengguo Wang , Linlin Mu , Guishan Ye , Kuijing He , Cong Cai , Peiyao Shi , Jieyu Zhou , Yaqin Gan , Yue Zeng , Anding Zhang , Long Li , Li Han\",\"doi\":\"10.1016/j.ijbiomac.2025.144800\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Canine distemper virus (CDV) is currently a significant viral disease that poses a threat to the health of pets and the breeding of fur-bearing animals. It is crucial to develop a diagnostic method that can be performed on-site, is simple to execute, and yields intuitively visible results. In this study, a neutralizing monoclonal antibody(mAb) 5-8H targeting the CDV-H protein was developed and characterized. The mAb 5-8H specifically recognizes prevalent CDV strains. The minimal linear epitopes recognized by 5-8H were identified as epitopes 498-607aa, with key amino acids being 531D, 552R, 554T, and 599R. These four key antigenic sites exhibited a high degree of conservation among all CDV strains, with conservatism ranging from 94.39 % to 99.78 %. The three-dimensional structural revealed that the antigenic epitope was exposed on the surface of the CDV-H protein, making it accessible for binding with antibody. Based on mAb 5-8H, a highly sensitive and specific colloidal gold test strip for detecting CDV was developed. This method achieves a concordance rate of 96 % with RT-qPCR and is suitable for rapid detection of CDV.</div></div>\",\"PeriodicalId\":333,\"journal\":{\"name\":\"International Journal of Biological Macromolecules\",\"volume\":\"316 \",\"pages\":\"Article 144800\"},\"PeriodicalIF\":8.5000,\"publicationDate\":\"2025-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Biological Macromolecules\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0141813025053528\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biological Macromolecules","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0141813025053528","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Development of a neutralizing monoclonal antibody recognizing a conserved epitope of CDV-H protein and its colloidal gold test strip for antigen detection
Canine distemper virus (CDV) is currently a significant viral disease that poses a threat to the health of pets and the breeding of fur-bearing animals. It is crucial to develop a diagnostic method that can be performed on-site, is simple to execute, and yields intuitively visible results. In this study, a neutralizing monoclonal antibody(mAb) 5-8H targeting the CDV-H protein was developed and characterized. The mAb 5-8H specifically recognizes prevalent CDV strains. The minimal linear epitopes recognized by 5-8H were identified as epitopes 498-607aa, with key amino acids being 531D, 552R, 554T, and 599R. These four key antigenic sites exhibited a high degree of conservation among all CDV strains, with conservatism ranging from 94.39 % to 99.78 %. The three-dimensional structural revealed that the antigenic epitope was exposed on the surface of the CDV-H protein, making it accessible for binding with antibody. Based on mAb 5-8H, a highly sensitive and specific colloidal gold test strip for detecting CDV was developed. This method achieves a concordance rate of 96 % with RT-qPCR and is suitable for rapid detection of CDV.
期刊介绍:
The International Journal of Biological Macromolecules is a well-established international journal dedicated to research on the chemical and biological aspects of natural macromolecules. Focusing on proteins, macromolecular carbohydrates, glycoproteins, proteoglycans, lignins, biological poly-acids, and nucleic acids, the journal presents the latest findings in molecular structure, properties, biological activities, interactions, modifications, and functional properties. Papers must offer new and novel insights, encompassing related model systems, structural conformational studies, theoretical developments, and analytical techniques. Each paper is required to primarily focus on at least one named biological macromolecule, reflected in the title, abstract, and text.