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The leader proteinase of foot-and-mouth disease virus: Efficiency through exosites
1Max Perutz Labs, Medical University of Vienna, Dept. of Medical Biochemistry, Dr. Bohr-Gasse 9/3, A-1030, Vienna, Austria.
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.
Insights
Foot-and-mouth disease virus leader proteinase (Lbpro) targets host proteins to aid viral replication. Lbpro utilizes unique interactions beyond substrate binding sites for efficient host cell manipulation.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Viral proteinases were discovered in the 1970s, initially thought solely for viral protein processing.
- Research revealed viral proteinases can alter host cell metabolism to enhance viral replication.
Purpose of the Study:
- To review the specific cellular targets of the foot-and-mouth disease virus (FMDV) leader proteinase (Lbpro).
- To illustrate how Lbpro uses non-canonical interactions to cleave host proteins for FMDV replication.
Main Methods:
- Literature review of studies on FMDV Lbpro.
- Analysis of protein-protein interactions and cleavage mechanisms.
Main Results:
- FMDV Lbpro cleaves specific cellular targets within the host.
- Lbpro employs interactions outside its active site to achieve targeted cleavage.
Conclusions:
- Viral proteinases, like FMDV Lbpro, have evolved sophisticated mechanisms to manipulate host cells.
- Understanding these interactions is crucial for developing antiviral strategies against FMDV.
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