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Expression and antigenicity characterization for truncated capsid protein of porcine circovirus type 2 Полный текст
2011
Lou, Zhongzi | Li, Xuerui | Li, Zhiyong | Yin, Xiangping | Li, Baoyu | Lan, Xi | Yang, Bin | Zhang, Yun | Liu, Jixing
Three pairs of specific primers were designed to amplify F2-1, F2-2, and XF2-2 truncated capsid protein genes of porcine circovirus type 2 (PCV-2). Amplified sequences were subcloned to pET-32a(+) vectors and expressed in Rosetta (DE3) Escherichia coli by induction of isopropy-β-D-thiogalactoside (IPTG). All of the fusion proteins had positive reactions to PCV-2 antiserum and His-XF2-2 showed the best reactivity. Proteins were used to immunize BALB/c mice to produce monoclonal antibodies (mAbs), and 7 mAbs were selected. Capsid protein N-terminal parts 55 to 96 amino acid (aa), 97 to 141 aa, and 143 to 211 aa were confirmed as binding regions of the 7 mAbs. Reactivity between His-XF2-2 and the 7 mAbs was detected, FmAb-8 showed the best reactivity. The dominant B-cell epitope was located at 97 to 141 aa. The PEPSCAN indicated that the P122–136 peptide contained the dominant B-cell epitope.
Показать больше [+] Меньше [-]Molecular evolution of porcine reproductive and respiratory syndrome virus in Guangxi of China from 2012 to 2015 Полный текст
2019
Song, M. (Qingdao Agricultural University, Qingdao (China). College of Veterinary Medicine) | Zhang, Q. | Shan, H. | Yu, B. | Xiong, Y. | Li, J.
Real-time PCR assay for rapid differentiation of env-based genotypes of feline leukemia virus Полный текст
2019
Nakagawa, S. (Iwate University, Morioka, Iwate (Japan). Faculty of Agriculture, Cooperative Department of Veterinary Medicine, Laboratory of Veterinary Microbiology) | Kitamura, Y. | Naito, I. | Kaneda, M. | Chiba, Y. | Shimamura, S. | Yamasaki, M. | Hikono, H. | Murakami, K.
