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Description

Thosea asigna virus (TaV), a member of the genus Betatetravirus of the family Tetraviridae, is a positive-sense single-stranded RNA virus that infects lepidopteran insects. This family is divided into the Betatetravirus and Omegatetravirus genera, based upon of the appearance of the virion and genome organization. 2A peptides and 2A-like peptide sequences (known as cis-acting hydrolase elements or CHYSEL) are a superior alternative to internal ribosomal entry sites (IRES) for coordinating the expression of multiple gene products from a single recombinant construct. The 2A sequences are relatively short peptides of about 16-20 amino acids (depending on the virus of origin). They contain a highly conserved sequence, GDVEXNPGP, at the C-terminus, which is shared by different 2As and is essential for the creation of steric hindrance and ribosome skipping. These peptides allow multiple proteins to be encoded as polyproteins, which then dissociate into component proteins upon translation. The 2A sequence impairs normal peptide bond formation via a mechanism called ribosomal skipping, which results in effective, non-enzymatic generation of distinct peptide products from a single multi-cistronic construct. These peptides are used by several families of viruses, the best-known amongst these are foot-and-mouth disease virus 2A (F2A) and Thosea asigna virus 2A (T2A). Clone 5E6 is a rat monoclonal antibody that reacts with a protein in lysate from HEK293T cells transfected with various 2A-tagged proteins.