Dissecting the Subcellular Localization, Intracellular Trafficking, Interactions, Membrane Association, and Topology of Citrus Leprosis Virus C Proteins

Author(s)

Leastro, Mikhail Oliveira ^[1] ; Kitajima, Elliot Watanabe ^[2] ; Silva, Marilia Santos ^[3] ; Resende, Renato Oliveira ^[4] ; Freitas-Astua, Juliana ^{[5, 1]}

Affiliation

^[1] Inst Biol, Dept Bioquim Fitopatol, Sao Paulo - Brazil

^[2] Univ Sao Paulo, Dept Fitopatol & Nematol, Escola Super Agr Luiz de Queiroz, Piracicaba - Brazil

^[3] Embrapa Recursos Genet & Biotecnol, Lab Bioimagem, Brasilia, DF - Brazil

^[4] Univ Brasilia, Dept Biol Celular, Brasilia, DF - Brazil

^[5] Embrapa Mandioca & Fruticultura, Cruz Das Almas, BA - Brazil

• Document type: Journal article
• Source: FRONTIERS IN PLANT SCIENCE; v. 9, SEP 11 2018.
• Web of Science Citations: 1

Abstract

Citrus leprosis (CL) is a re-emergent viral disease affecting citrus crops in the Americas, and citrus leprosis virus C (CiLV-C), belonging to the genus Cilevirus, is the main pathogen responsible for the disease. Despite the economic importance of CL to the citrus industry, very little is known about the performance of viral proteins. Here, we present a robust in vivo study around functionality of p29, p15, p61, MP, and p24 CiLV-C proteins in the host cells. The intracellular sub-localization of all those viral proteins in plant cells are shown, and their co-localization with the endoplasmic reticulum (ER), Golgi complex (GC) ( p15, MP, p61 and p24), actin filaments (p29, p15 and p24), nucleus (p15), and plasmodesmata (MP) are described. Several features are disclosed, including i) ER remodeling and redistribution of GC apparatus, ii) trafficking of the p29 and MP along the ER network system, iii) self-interaction of the p29, p15, and p24 and hetero-association between p29-p15, p29-MP, p29-p24, and p15-MP proteins in vivo. We also showed that all proteins are associated with biological membranes; whilst p15 is peripherally associated, p29, p24, and MP are integrally bound to cell membranes. Furthermore, while p24 exposes an N-cytoplasm-C-lumen topology, p29, and p15 are oriented toward the cytoplasmic face of the biological membrane. Based on our findings, we discuss the possible performance of each protein in the context of infection and a hypothetical model encompassing the virus spread and sites for replication and particle assembly is suggested. (AU)

• FAPESP's process: 15/10249-1 - Studies of infective processes of Citrus leprosis virus (CiLV-C), with emphasis in the construction of infectious clone and characterization of viral proteins.
• Grantee: Mikhail Oliveira Leastro
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 14/08458-9 - Plant viruses transmitted by Brevipalpus mites (Acari: Tenuipalpidae) - BTV: survey, identification, molecular characterization, phylogeny; virus/vector/host relationhip; biology, taxonomy and management of the mite
• Grantee: Elliot Watanabe Kitajima
• Support Opportunities: Research Projects - Thematic Grants