Characterisation of novel linear antigen epitopes on North American-type porcine reproductive and respiratory syndrome virus M protein
文献类型: 外文期刊
第一作者: Wang, Qian
作者: Wang, Qian;Guo, Xin;Ge, Xinna;Yang, Hanchun;Wang, Qian;Guo, Xin;Ge, Xinna;Yang, Hanchun;Wang, Qian;Chen, Jiazeng;Peng, Jinmei;An, Tongqing;Leng, Chaoliang;Sun, Yan;Tian, Zhijun
作者机构:
期刊名称:ARCHIVES OF VIROLOGY ( 影响因子:2.574; 五年影响因子:2.466 )
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年卷期:
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收录情况: SCI
摘要: The M protein, encoded by the porcine reproductive and respiratory syndrome virus (PRRSV) ORF6 gene, is considered to be one of the most conserved PRRSV proteins. In recent decades, highly specific monoclonal antibodies (Mabs) have been exploited to provide reliable diagnoses for many diseases. In this study, two different Mab clones targeting the linear epitopes on the PRRSV M protein were generated and characterized. Both Mabs showed binding activity against the native PRRSV virion and recombinant M protein when analyzed by immunofluorescence assay (IFA) and Western blot. The targeted epitope of each Mab was mapped by serial truncation of the M protein to generate overlapping fragments. Fine epitope mapping was then performed using a panel of expressed polypeptides. The polypeptide sequences of the two epitopes recognized by Mabs 1C8 and 3F7 were 3SSLD6 and 155VLGGRKAVK163, respectively, with the former being a newly identified epitope on the M protein. In both cases, these two epitopes were finely mapped for the first time. Alignments of Mab epitope sequences revealed that the two epitopes on the M protein were highly conserved between the North American-type strains. These Mabs, along with their mapped epitopes, are useful for the development of diagnostic and research tools, including immunofluorescence, ELISA and Western blot.
分类号: R37
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