Abstract
Viroporins are involved in viral pathogenesis, play an important role in the morphogenesis of virions and ensure their release from the infected cell. These proteins are potentially promising as possible targets for the regulation of virus reproduction. The literature data on the current understanding of coronavirus viroporins functioning are summarized in the review. Special attention is focused on specific structural features that determine the functional ability of these proteins. The basic principles of viroporins localization in the cell and their influence on the coronavirus life cycle are considered. Keywords: coronavirus, pore formation, protein 3a, protein 8a, protein E, SARS, viroporins
Highlights
Viroporins are small hydrophobic virusinduced proteins capable to modify cellular permeability for ions or other small molecules when interacting with membranes
Viroporins genes have been found in variousviral genomes, they are most often described for RNA-containing viruses, including a number of human pathogens: hepatitis C virus (HCV), HIV1 (HIV-1), influenza virus, poliomyelitis virus, and others, including coronavirus severe acute respiratory syndrome (SARS)-CoV [7]
It is interesting that recent studies of the protein 3a SARS CoV-2 structure showed a high level of its similarity (97.82%) by amino acid sequence with the structural protein NS3 of the bat coronavirus RaTG13, which may be another confirmation of the zoonotic origin of COVID-19 [22]
Summary
The coronavirus genome encodes 4 main structural proteins (Fig. 1): E - envelope protein, M membrane protein, N – nucleocapsid protein, and S spikes protein [8]. The results clearly indicate that epitope labels do not affect the location of this protein in the cell: regardless of the concentration and mode of protein E expression, its prevailing amount is localized in EP and AG Considering this trend, the search for the region of protein E molecule, which is informatively responsible for targeting on ERGIC, is obviously promising in the aspect of preventing the development of viral infection. Based on the sequence of the SARS coronavirus genome and phylogenetic analysis, similar binding centers of cysteine nature were found in proteins E and S: in protein E, this structure was located directly next to the transmembrane domain, but in S - at the carboxyl end of the molecule. The study of the mechanisms of structural proteins of the envelope of other representatives of coronaviruses is interesting from a purely scientific point of view and promisingin terms of finding effective therapeutic pathways for the treatment of coronavirus diseases
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