Isolation and characterization of porcine monoclonal antibodies revealed two distinct serotype-independent epitopes on VP2 of foot-and-mouth disease virus
| العنوان: | Isolation and characterization of porcine monoclonal antibodies revealed two distinct serotype-independent epitopes on VP2 of foot-and-mouth disease virus |
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| المؤلفون: | Zaixin Liu, Xueqing Ma, Yuanfang Fu, Yimei Cao, Shasha Zhou, Yingli Chen, Guoqiang Zhu, Huifang Bao, Hengmei Wang, Dong Li, Zengjun Lu, Jing Zhang, Pu Sun, Pinghua Li, Xingwen Bai, Kun Li |
| المصدر: | Journal of General Virology. 102 |
| بيانات النشر: | Microbiology Society, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | 0301 basic medicine, Swine, medicine.drug_class, Genes, Immunoglobulin Heavy Chain, viruses, 030106 microbiology, Antibody Affinity, Antibodies, Viral, Serogroup, Immunoglobulin light chain, Monoclonal antibody, Epitope, Epitopes, 03 medical and health sciences, Antigen, Virology, medicine, Animals, Antigens, Viral, B-Lymphocytes, Linear epitope, biology, Antibodies, Monoclonal, virus diseases, biochemical phenomena, metabolism, and nutrition, biology.organism_classification, 030104 developmental biology, Foot-and-Mouth Disease Virus, Immunoglobulin G, biology.protein, Capsid Proteins, Immunoglobulin Light Chains, Genes, Immunoglobulin Light Chain, Foot-and-mouth disease virus, Antibody, Immunoglobulin Heavy Chains, Epitope Mapping, Conformational epitope |
| الوصف: | Pigs are susceptible to foot-and-mouth disease virus (FMDV), and the humoral immune response plays an essential role in protection against FMDV infection. However, little information is available about FMDV-specific mAbs derived from single B cells of pigs. This study aimed to determine the antigenic features of FMDV that are recognized by antibodies from pigs. Therefore, a panel of pig-derived mAbs against FMDV were developed using fluorescence-based single B cell antibody technology. Western blotting revealed that three of the antibodies (1C6, P2-7E and P2-8G) recognized conserved antigen epitopes on capsid protein VP2, and exhibited broad reactivity against both FMDV serotypes A and O. An alanine-substitution scanning assay and sequence conservation analysis elucidated that these porcine mAbs recognized two conserved epitopes on VP2: a linear epitope (2KKTEETTLL10) in the N terminus and a conformational epitope involving residues K63, H65, L66, F67, D68 and L81 on two β-sheets (B-sheet and C-sheet) that depended on the integrity of VP2. Random parings of heavy and light chains of the IgGs confirmed that the heavy chain is predominantly involved in binding to antigen. The light chain of porcine IgG contributes to the binding affinity toward an antigen and may function as a support platform for antibody stability. In summary, this study is the first to reveal the conserved antigenic profile of FMDV recognized by porcine B cells and provides a novel method for analysing the antibody response against FMDV in its natural hosts (i.e. pigs) at the clonal level. |
| تدمد: | 1465-2099 0022-1317 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaa6f1ee3e4a63b3625ea322a67f702bTest https://doi.org/10.1099/jgv.0.001608Test |
| رقم الانضمام: | edsair.doi.dedup.....aaa6f1ee3e4a63b3625ea322a67f702b |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14652099 00221317 |
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