A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for the begomovirus CabLCV.

Autor:	Gouveia-Mageste BC; National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil., Martins LGC; National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil., Dal-Bianco M; National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.; Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil., Machado JPB; National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.; Agronomy Institute, Universidade Federal de Viçosa, Campus Florestal, Florestal, Minas Gerais 35690-000, Brazil., da Silva JCF; National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil., Kim AY; Genomic Analysis Laboratory, Plant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037, USA., Yazaki J; Genomic Analysis Laboratory, Plant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037, USA.; RIKEN Center for Integrative Medical Sciences, Yokohama City, Kanagawa 230-0045, Japan., Dos Santos AA; National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.; Departament of General Biology, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil., Ecker JR; Howard Hughes Medical Institute and Plant Biology Laboratory, The Salk Institute of Biological Studies, La Jolla, California 92037, USA., Fontes EPB; National Institute of Science and Technology in Plant-Pest Interactions, Bioagro, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.; Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-000, Brazil.
Jazyk:	angličtina
Zdroj:	Plant physiology [Plant Physiol] 2021 Sep 04; Vol. 187 (1), pp. 158-173.
DOI:	10.1093/plphys/kiab252
Abstrakt:	Because of limited free diffusion in the cytoplasm, viruses must use active transport mechanisms to move intracellularly. Nevertheless, how the plant single-stranded DNA begomoviruses hijack the host intracytoplasmic transport machinery to move from the nucleus to the plasmodesmata remains enigmatic. Here, we identified nuclear shuttle protein (NSP)-interacting proteins from Arabidopsis (Arabidopsis thaliana) by probing a protein microarray and demonstrated that the cabbage leaf curl virus NSP, a facilitator of the nucleocytoplasmic trafficking of viral (v)DNA, interacts in planta with an endosomal vesicle-localized, plant-specific syntaxin-6 protein, designated NSP-interacting syntaxin domain-containing protein (NISP). NISP displays a proviral function, unlike the syntaxin-6 paralog AT2G18860 that failed to interact with NSP. Consistent with these findings, nisp-1 mutant plants were less susceptible to begomovirus infection, a phenotype reversed by NISP complementation. NISP-overexpressing lines accumulated higher levels of vDNA than wild-type. Furthermore, NISP interacted with an NSP-interacting GTPase (NIG) involved in NSP-vDNA nucleocytoplasmic translocation. The NISP-NIG interaction was enhanced by NSP. We also showed that endosomal NISP associates with vDNA. NISP may function as a docking site for recruiting NIG and NSP into endosomes, providing a mechanism for the intracytoplasmic translocation of the NSP-vDNA complex toward and from the cell periphery. (© American Society of Plant Biologists 2021. All rights reserved. For permissions, please email: journals.permissions@oup.com.)
Databáze:	MEDLINE
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