A Capsid Protein Fragment of a Fusagra-like Virus Found in Carica papaya Latex Interacts with the 50S Ribosomal Protein L17

• Published in: Viruses 2023-02, Vol.15 (2), p.541
• Main Authors: Maurastoni, Marlonni, Sá Antunes, Tathiana F, Abreu, Emanuel F M, Ribeiro, Simone G, Mehta, Angela, Sanches, Marcio M, Fontes, Wagner, Kitajima, Elliot W, Cruz, Fabiano T, Santos, Alexandre M C, Ventura, Jose A, Gomes, Ana C M M, Zerbini, F Murilo, Sosa-Acosta, Patricia, Nogueira, Fábio C S, Rodrigues, Silas P, Aragão, Francisco J L, Whitfield, Anna E, Fernandes, Patricia M B
• Format: Article
• Language: English
• Subjects: Amino Acids; Biodegradation; Capsid; Capsid protein; Capsid Proteins - genetics; Carica; Carica papaya; Chromatography, Liquid; coat protein; dsRNA; fusagra-like virus; Gel electrophoresis; Genomes; Latex; Mass spectrometry; Peptides; Plant cells; plant virus; Proteins; protein–protein interaction; Proteolysis; Ribosomal protein L17; RNA polymerase; RNA Viruses - genetics; Scientific imaging; Sodium; Sodium lauryl sulfate; Sticky disease; Structural proteins; Sucrose; Tandem Mass Spectrometry; Totiviridae; Virions; Viruses
• ISSN: 1999-4915; 1999-4915
• DOI: 10.3390/v15020541

Papaya sticky disease is caused by the association of a fusagra-like and an umbra-like virus, named papaya meleira virus (PMeV) and papaya meleira virus 2 (PMeV2), respectively. Both viral genomes are encapsidated in particles formed by the PMeV ORF1 product, which has the potential to encode a protein with 1563 amino acids (aa). However, the structural components of the viral capsid are unknown. To characterize the structural proteins of PMeV and PMeV2, virions were purified from latex. SDS-PAGE analysis of purified virus revealed two major proteins of ~40 kDa and ~55 kDa. Amino-terminal sequencing of the ~55 kDa protein and LC-MS/MS of purified virions indicated that this protein starts at aa 263 of the deduced ORF1 product as a result of either degradation or proteolytic processing. A yeast two-hybrid assay was used to identify proteins interacting with two PMeV ORF1 product fragments (aa 321-670 and 961-1200). The 50S ribosomal protein L17 ( RPL17) was identified as potentially associated with modulated translation-related proteins. In plant cells, RPL17 co-localized and interacted with the PMeV ORF1 fragments. These findings support the hypothesis that the interaction between PMeV/PMeV2 structural proteins and RPL17 is important for virus-host interactions.