Generation and epitope mapping of novel neutralizing monoclonal antibodies against glycoprotein E2 of CSFV

文献类型： 外文期刊

第一作者： Mi, Shijiang

作者： Mi, Shijiang;Tu, Changchun;Bao, Fei;Liu, Zhongdi;Zhang, Yixiao;Tu, Changchun;Gong, Wenjie;Li, Hongwei;Wu, Meng;Tu, Changchun

作者机构：

关键词： Classical swine fever virus; E2 protein; Neutralizing mAb; Characterization; Epitope mapping

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）

ISSN： 0141-8130

年卷期： 2024 年 282 卷

页码：

收录情况： SCI

摘要： Classical swine fever virus (CSFV) is a highly contagious and economically important pathogen threatening pig industry worldwide, the envelope glycoprotein E2 of CSFV is the dominant antigen inducing strong antiviral neutralizing immunity. In this study, 7 monoclonal antibodies (mAbs) with neutralizing potency were generated using E2 protein of CSFV Shimen strain (SM) expressed by eukaryotic cells. Their reactivity with 116 CSFV strains in cell cultures and E2 proteins of 10 subgenotypes in western blots showed different CSFV spectrums they recognized. Of them, three (HCL-001, HCL-005 and HCL-010) reacted with all CSFV subgenotypes, while HCL014 and HCL-002 reacted with most CSFV strains, except for some variants in genotype 2.3. In contrast, mAb HCL-009 reacted only with a few subgenotype 1.1 strains including SM, field strains and some vaccine strains. Interestingly, mAb HCL-018 reacted only with SM and field subgenotype 1.1 strains, not with any vaccine strains. Further epitope mapping using chimeric and site-directed mutated E2 proteins showed that HCL-001, HCL-005 and HCL-010 recognized a conservative epitope motif 143SPT145,L147, and HCL-002 recognized a conformational epitope with key aa motifs of 95 GDD 97 , 157 RX(D/E)K( R )XFXXR 164 . HCL-014 recognized a new conservative epitope with key aa motifs of 41 D, 58 XNVVXRR 64 . HCL-009 and HCL-018 recognized the epitope with key aa motifs of 36D,40ND41,45KXI47 and 69 LHXGXLLT 76 , respectively. Taken together, present study has provided not only new insights into the antigenic structure of E2 protein, but also key reagents for antigenic characterization of CSFV strains and development of antibody assay for evaluation of the vaccination efficacy.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序