2A and 2A-Like Sequences in Viruses: Function, Mechanism and Biotechnological/Biomedical Applications
A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "General Virology".
Deadline for manuscript submissions: 31 October 2026 | Viewed by 48
Special Issue Editors
Interests: picornaviruses; virus-encoded proteinases; translation; biotechnolgy
Special Issue Information
Dear Colleagues,
The Picornavirus 2A polyprotein region is by far the most plastic region amongst the various genera in the family. Whilst in some genera this region is composed of multiple different 2A proteins, in the Aphthovirus Foot-and-Mouth Disease Virus (FMDV), 2A is an oligopeptide and is only 18aa long. Early analyses revealed two crucial features: (i) the co-translational ‘cleavage’ occurred between the C-terminal glycine of FMDV 2A and the N-terminal proline of FMDV 2B (-NPG↓P-) and (ii) 2A was an autonomous element, which refers to an in-frame insertion of the 18aa 2A (together with the N-terminal proline of FMDV 2B) between the green fluorescent protein (GFP: stop codon removed) and β-glucuronidase (GUS). This created a [GFP2AGUS] synthetic polyprotein which showed high-level (>90%) co-translational ‘cleavage’, producing [GFP2A] and GUS. The latter observation opened up a new biotechnology for the co-expression of multiple proteins within a single cell and from a single promoter. Latterly, bioinformatic analyses have shown the presence of “2A-like” sequences in a wide range of virus genomes and within certain cellular sequences.
In this Special Issue, papers will discuss the occurrence and function of 2A-like sequences in virus genomes, cellular 2A-like sequences, the mechanism of 2A-mediated “cleavage”, the use of 2A in biotechnology, and the use of 2A in biomedicine.
Prof. Dr. Martin Ryan
Dr. Garry Luke
Guest Editors
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Keywords
- virus protein biogenesis
- ribosome ‘skipping’
- protein co-expression
- biotechnology
- biomedicine
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