3C-like proteases at the interface of plant-virus-vector interactions: Focus on potyvirid NIa proteases and secovirid proteases.

Autor: Sanfaçon H; Summerland Research and Development Centre, Agriculture and Agri-Food Canada, 4200 Highway 97, V0H 1Z0, Summerland, BC, Canada. Electronic address: helene.sanfacon@agr.gc.ca.
Jazyk: angličtina
Zdroj: Virology [Virology] 2025 Jan; Vol. 602, pp. 110299. Date of Electronic Publication: 2024 Nov 14.
DOI: 10.1016/j.virol.2024.110299
Abstrakt: Plant viruses of the families Potyviridae and Secoviridae encode 3C-like proteases (3CL pro ) that are related to picornavirus 3C proteases. This review discusses recent advances in deciphering the multifunctional activities of plant virus 3CL pro . These proteases regulate viral polyprotein processing and facilitate virus replication. They are also determinants of host range, virulence, symptomatology and super-infection exclusion in some plant-virus interactions and facilitate aphid transmission. Potyvirid NIa-Pro proteases interact with host factors to interfere with a variety of defense mechanisms: salicylic acid-dependent signaling, ethylene-dependent signaling, transcriptional gene silencing and RNA decay. Potyvirid NIa-Pro also cleave host proteins at signature cleavage sites, although the biological impact of these cleavage remains to be determined. Recently, a plant defense mechanism was uncovered that inhibits the proteolytic activity of a comovirus 3CL pro . Future perspectives are discussed including using proteomic and degradomic techniques to elucidate the network of interactions of plant virus 3CL pro with the host proteome.
Competing Interests: Declaration of competing interest I have nothing to declare.
(Crown Copyright © 2024. Published by Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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