The leader proteinase of foot-and-mouth disease virus: Efficiency through exosites

IF 2.4 3区 医学 Q3 VIROLOGY Virology Pub Date : 2025-01-24 DOI:10.1016/j.virol.2025.110420
Tim Skern
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Abstract

Viruses were shown to encode proteinases in the 1970s. Initially, it was assumed that they would be only used for proteolytic processing of the viral proteins. Subsequent investigations showed that such proteinases could affect host metabolism to benefit viral replication. The foot-and-mouth disease virus (FMDV) leader proteinase (Lbpro) cleaves several specific cellular targets. This mini-review summarises the cellular targets of Lbpro and illustrates the protein interactions away from the canonical substrate binding sites that Lbpro has evolved to enable specific and efficient cleavage of host proteins to promote FMDV replication.
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口蹄疫病毒的先导蛋白酶:通过外来物的效率。
20 世纪 70 年代,病毒被证明编码蛋白酶。起初,人们认为这些蛋白酶只用于病毒蛋白质的蛋白水解处理。随后的研究表明,这些蛋白酶可以影响宿主的新陈代谢,从而有利于病毒的复制。口蹄疫病毒(FMDV)头蛋白酶(Lbpro)可裂解多个特定的细胞靶标。这篇微型综述总结了 Lbpro 的细胞靶标,并说明了 Lbpro 在经典底物结合位点之外的蛋白质相互作用,从而能够特异、高效地裂解宿主蛋白质,促进 FMDV 复制。
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来源期刊
Virology
Virology 医学-病毒学
CiteScore
6.00
自引率
0.00%
发文量
157
审稿时长
50 days
期刊介绍: Launched in 1955, Virology is a broad and inclusive journal that welcomes submissions on all aspects of virology including plant, animal, microbial and human viruses. The journal publishes basic research as well as pre-clinical and clinical studies of vaccines, anti-viral drugs and their development, anti-viral therapies, and computational studies of virus infections. Any submission that is of broad interest to the community of virologists/vaccinologists and reporting scientifically accurate and valuable research will be considered for publication, including negative findings and multidisciplinary work.Virology is open to reviews, research manuscripts, short communication, registered reports as well as follow-up manuscripts.
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