{"title":"[抗sars - cov -2中和性单克隆抗体与针对抗体治疗的变异交叉有效的分离]。","authors":"","doi":"10.2222/jsv.71.163","DOIUrl":null,"url":null,"abstract":"<p><p>We isolated five mAbs with potent neutralizing activities against SARS-CoV-2 from two convalescent COVID-19 patients infected with prototype virus. Among them, the 9-105 antibody that have a highest affinity for the receptor-binding domain (RBD), cross-neutralize variants, such as B.1.1.7 (alfa), mink cluster 5 variant, B.1.351 (beta), P.1 (gamma), C.37 (lambda), B.1.617.1 (kappa), B.1.617.2 (delta) and B.1.621 (mu). A single amino acid mutation at K417 of RBD decreased neutralization sensitivity of 9-105. A 9-105 homology model revealed that 9-105 light chain binds to RBD including K417 by the same angle as ACE2.</p>","PeriodicalId":75275,"journal":{"name":"Uirusu","volume":"71 2","pages":"163-168"},"PeriodicalIF":0.0000,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Isolation of anti-SARS-CoV-2 neutralizing monoclonal antibodies cross effective to variants aiming at antibody therapy].\",\"authors\":\"\",\"doi\":\"10.2222/jsv.71.163\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>We isolated five mAbs with potent neutralizing activities against SARS-CoV-2 from two convalescent COVID-19 patients infected with prototype virus. Among them, the 9-105 antibody that have a highest affinity for the receptor-binding domain (RBD), cross-neutralize variants, such as B.1.1.7 (alfa), mink cluster 5 variant, B.1.351 (beta), P.1 (gamma), C.37 (lambda), B.1.617.1 (kappa), B.1.617.2 (delta) and B.1.621 (mu). A single amino acid mutation at K417 of RBD decreased neutralization sensitivity of 9-105. A 9-105 homology model revealed that 9-105 light chain binds to RBD including K417 by the same angle as ACE2.</p>\",\"PeriodicalId\":75275,\"journal\":{\"name\":\"Uirusu\",\"volume\":\"71 2\",\"pages\":\"163-168\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2021-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Uirusu\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.2222/jsv.71.163\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Uirusu","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2222/jsv.71.163","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[Isolation of anti-SARS-CoV-2 neutralizing monoclonal antibodies cross effective to variants aiming at antibody therapy].
We isolated five mAbs with potent neutralizing activities against SARS-CoV-2 from two convalescent COVID-19 patients infected with prototype virus. Among them, the 9-105 antibody that have a highest affinity for the receptor-binding domain (RBD), cross-neutralize variants, such as B.1.1.7 (alfa), mink cluster 5 variant, B.1.351 (beta), P.1 (gamma), C.37 (lambda), B.1.617.1 (kappa), B.1.617.2 (delta) and B.1.621 (mu). A single amino acid mutation at K417 of RBD decreased neutralization sensitivity of 9-105. A 9-105 homology model revealed that 9-105 light chain binds to RBD including K417 by the same angle as ACE2.