Quarterly Reviews of Biophysics, Journal Year: 2025, Volume and Issue: 58
Published: Jan. 1, 2025
Abstract The ‘Viroporin’ family comprises a number of mostly small-sized, integral membrane proteins encoded by animal and plant viruses. Despite their sequence structural diversity, viroporins share common functional trend: capacity to assemble transmembrane channels during the replication cycle virus. Their selectivity spectrum ranges from low-pH-activated, unidirectional proton transporters, size-limited permeating pores allowing passive diffusion metabolites. Through mechanisms not fully understood, expression facilitates virion assembly/release infected cells, subverts cell physiology, contributing cytopathogenicity. Compounds that interact with interfere membrane-permeabilizing activity in vitro , are known inhibit virus production. Moreover, viroporin-defective viruses comprise source live attenuated vaccines prevent infection notorious human livestock pathogens. This review dives into origin evolution viroporin concept, summarizes some methodologies used characterize structure–function relationships these important virulence factors, attempts classify them on biophysical grounds attending ion/solute transport across membranes.
Language: Английский