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Viroporin

The transmembrane helical tetramer of the influenza A virus M2 protein, which functions as a proton channel, in complex with the channel-blocking drug amantadine (shown in red). Highly conserved tryptophan and histidine residues known to play key roles in mediating proton transport are shown as sticks. From PDB: 3C9J​.[1]

Viroporins are small and usually hydrophobic multifunctional viral proteins that modify cellular membranes, thereby facilitating virus release from infected cells.[2][3] Viroporins are capable of assembling into oligomeric ion channels or pores in the host cell's membrane, rendering it more permeable and thus facilitating the exit of virions from the cell. Many viroporins also have additional effects on cellular metabolism and homeostasis mediated by protein-protein interactions with host cell proteins.[3] Viroporins are not necessarily essential for viral replication, but do enhance growth rates. They are found in a variety of viral genomes but are particularly common in RNA viruses. Many viruses that cause human disease express viroporins. These viruses include hepatitis C virus, HIV-1, influenza A virus, poliovirus, respiratory syncytial virus, and SARS-CoV.[3][4][5]

  1. ^ Thomaston JL, Alfonso-Prieto M, Woldeyes RA, Fraser JS, Klein ML, Fiorin G, DeGrado WF (November 2015). "High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction". Proceedings of the National Academy of Sciences of the United States of America. 112 (46): 14260–5. Bibcode:2015PNAS..11214260T. doi:10.1073/pnas.1518493112. PMC 4655559. PMID 26578770.
  2. ^ Carrasco L (August 1995). "Modification of membrane permeability by animal viruses". Advances in Virus Research. 45: 61–112. doi:10.1016/S0065-3527(08)60058-5. ISBN 9780120398454. PMC 7131156. PMID 7793329.
  3. ^ a b c Gonzalez ME, Carrasco L (September 2003). "Viroporins". FEBS Letters. 552 (1): 28–34. doi:10.1016/S0014-5793(03)00780-4. hdl:20.500.12105/7778. PMID 12972148. S2CID 209557930.
  4. ^ Nieto-Torres JL, Verdiá-Báguena C, Castaño-Rodriguez C, Aguilella VM, Enjuanes L (July 2015). "Relevance of Viroporin Ion Channel Activity on Viral Replication and Pathogenesis". Viruses. 7 (7): 3552–73. doi:10.3390/v7072786. PMC 4517115. PMID 26151305.
  5. ^ Nieva JL, Madan V, Carrasco L (July 2012). "Viroporins: structure and biological functions". Nature Reviews. Microbiology. 10 (8): 563–74. doi:10.1038/nrmicro2820. PMC 7097105. PMID 22751485.

Viroporin

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