Abstract

2A is an oligopeptide sequence that mediates a ribosome “skipping” effect and can mediate a co-translation cleavage of polyproteins. These sequences are widely distributed from insect to mammalian viruses and could act by accelerating adaptive capacity. These sequences have been used in many heterologous co-expression systems because they are versatile tools for cleaving proteins of biotechnological interest. In this work, we review and update the occurrence of 2A/2A-like sequences in different groups of viruses by screening the sequences available in the National Center for Biotechnology Information database. Interestingly, we reported the occurrence of 2A-like for the first time in 69 sequences. Among these, 62 corresponded to positive single-stranded RNA species, six to double stranded RNA viruses, and one to a negative-sense single-stranded RNA virus. The importance of these sequences for viral evolution and their potential in biotechnological applications are also discussed.

Highlights

  • An active search was performed on the publication linked to the sequence annotation in the National Center for Biotechnology Information (NCBI) database to identify whether the sequences found had already been reported in the literature after the initial screening

  • Luke et al were the first to report this wide distribution and identified motifs similar to those found in the foot-and-mouth disease virus (FMDV) [2]

  • Because of its cleavage function, the 2A/2A-like sequences appear to directly affect the complexity of the viral genome, which plays a decisive role in viral evolution

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Summary

Introduction

During amino acid insertion into the protein, the 2A sequence can cause a structural modification at the ribosome peptidyl-transferase center (PTC), making the ribosome “skip” the proline codon It inhibits the formation of a glycineproline peptide bond because of the hydrolysis of the peptidyl (2A)-tRNAGly ester linkage, releasing the polypeptide from the translational complex [3,4]. In this way, the first amino acid, proline, of the downstream encoded protein, is specified by the third codon in the sequence of P7 G8 P9 , and the C-terminal amino acid of the upstream encoded protein is a glycine encoded by the second codon in that sequence [5,6].

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