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Beschreibung

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 20 amino acids (depending on the virus of origin) containing the consensus motif Asp-Val/Ile-Glu-X-Asn-Pro-Gly-Pro. 2A 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 multicistronic construct. 2A peptides are used by several families of viruses, the best known foot-and-mouth disease virus of the Picornaviridae family, for producing multiple polypeptides. Anti-2A peptide, clone 3H4 recognizes 2A sequence derived from foot and mouth piconavirus (VKQTLNFDLLKLAGDVESNPG*P) with cleavage site between G and P. (Ref.: Trichas, G, et al. (2008). BMC Biol. 6: 40).