2A

2Apeptide sequenceswere found in Picornaviruses to mediate "cleavage" between two proteins.We use 2A peptide-linked multicistronic vectors to express multiple proteins from a single open reading frame (ORF)effectively.
The 18~22 amino acids 2A self-cleaving oligopeptidescan be used for co-expression ofmultiple, discrete proteins from a single ORF.Based on highly inefficient peptide bond formation between glycineand proline residues within the 2A peptide, placementof 2A peptide sequence as a linker region betweentandem cDNA’s allows the stoichiometric translation ofmultiple unfused protein products.These sequences were first discovered in the foot-and-mouth disease virus (FMDV).And since than many 2A-like sequences have been identified in other viruses and some parasites.To minimize therisk of homologous recombination, it is important to use different 2A peptide sequences if morethan two genes are being linked.The 2A peptide system has thus far worked successfully in all eukaryotic systems tested, from mammaliancells, yeast, and plants.In our project,we use F2A(from foot-and-mouth disease virus), P2A(from porcine teschovirus-1) and T2A(fromThosea asigna virus) to achieve our goal.

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