数字农科院2.0

Function investigation of p11.5 in ASFV infection

文献类型： 外文期刊

作者： Yin, Dan;Shi, Bin;Geng, Renhao;Liu, Yingnan;Gong, Lang;Shao, Hongxia;Qian, Kun;Chen, Hongjun;Qin, Aijian

作者机构：

关键词： African swine fever virus;p72 protein;p11.5 protein;Protein interactions

期刊名称： VIROLOGICA SINICA

ISSN： 1674-0769

年卷期： 2024 年 39 卷 3 期

页码：

收录情况： SCIE（2024版） ; ; CSCD（2023-2024年度） ; ; 科技核心（2024版）

摘要： Virus replication relies on complex interactions between viral proteins. In the case of African swine fever virus (ASFV), only a few such interactions have been identi fied so far. In this study, we demonstrate that ASFV protein p72 interacts with p11.5 using co-immunoprecipitation and liquid chromatography-mass spectrometry (LC-MS). It was found that protein p72 interacts speci fically with p11.5 at sites amino acids (aa) 1 -216 of p72 and aa 1 -68 of p11.5. To assess the importance of p11.5 in ASFV infection, we developed a recombinant virus (ASFVGZ Delta A137R) by deleting the A137R gene from the ASFVGZ genome. Compared with ASFVGZ, the infectious progeny virus titers of ASFVGZ Delta A137R were reduced by approximately 1.0 logs. In addition, we demonstrated that the growth defect was partially attributable to a higher genome copies-to-infectious virus titer ratios produced in ASFVGZ Delta A137R-infected MA104 cells than in those infected with ASFVGZ. This finding suggests that MA104 cells infected with ASFVGZ Delta A137R may generate larger quantities of noninfectious particles. Importantly, we found that p11.5 did not affect virus-cell binding or endocytosis. Collectively, we show for the first time the interaction between ASFV p72 and p11.5. Our results effectively provide the relevant information of the p11.5 protein. These results extend our understanding of complex interactions between viral proteins, paving the way for further studies of the potential mechanisms and pathogenesis of ASFV infection.

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