Nonstructural p26 proteins encoded by the 3’-proximal genes of velariviruses and criniviruses are orthologs

• Published in: Archives of virology Vol. 165; no. 2; pp. 439 - 443
• Main Authors: Rogozin, I. B., Agranovsky, A. A.
• Format: Journal Article
• Language: English
• Published: Vienna Springer Vienna 01.02.2020; Springer Nature B.V
• Subjects: Amino Acid Sequence; Biomedical and Life Sciences; Biomedicine; Brief Report; Closteroviridae - genetics; Conserved sequence; Crinivirus - genetics; Genome, Viral - genetics; Genomes; Infectious Diseases; Medical Microbiology; Nucleotide sequence; Phylogeny; Plant virus diseases; Proteins; Ribonucleic acid; RNA; RNA, Viral - genetics; Sequence Alignment; Sequence analysis; Structural proteins; Viral Proteins - genetics; Virology
• ISSN: 0304-8608; 1432-8798
• DOI: 10.1007/s00705-019-04491-8

The 3’-most genes in RNA-2 of the Crinivirus genus members (family Closteroviridae ) code for non-structural p26 proteins that share amino acid sequence similarity [Stewart LR, Hwang MS, Falk BW (2009) Virus Res 145:293-299]. In this study, sensitive bioinformatic tools have been used to identify the homologous p26 proteins encoded by the 3’ genes in monopartite genomes of the members of Velarivirus , another Closteroviridae genus, and mint vein banding-associated virus, an unassigned member of the family. The p26 proteins showed similarity in their predicted secondary structures, but an amino acid sequence alignment showed no strictly conserved positions, thus indicating a high plasticity of these non-structural proteins. The implications of the sequence analysis for possible functions of the crinivirus and velarivirus p26 proteins are discussed.