Constancy and diversity in the flavivirus fusion peptide.docVIP

Virology Journal BioMedCentral Research Open Access Constancy and diversity in the flavivirus fusion peptide Stephen J Seligman Address: Department of Microbiology and Immunology, New York Medical College, Valhalla, New York, USA Email: Stephen J Seligman - stephen_seligman@ Published: 14 February 2008 Received: 25 January 2008 Accepted: 14 February 2008 Virology Journal 2008, 5:27 doi:10.1186/1743-422X-5-27 This article is available from: /content/5/1/27 ? 2008 Seligman; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract Background: Flaviviruses include the mosquito-borne dengue, Japanese encephalitis, yellow fever and West Nile and the tick-borne encephalitis viruses. They are responsible for considerable world-wide morbidity and mortality. Viral entry is mediated by a conserved fusion peptide containing 16 amino acids located in domain II of the envelope protein E. Highly orchestrated conformational changes initiated by exposure to acidic pH accompany the fusion process and are important factors limiting amino acid changes in the fusion peptide that still permit fusion with host cell membranes in both arthropod and vertebrate hosts. The cell-fusing related agents, growing only in mosquitoes or insect cell lines, possess a different homologous peptide. Results: Analysis of 46 named flaviviruses deposited in the Entrez Nucleotides database extended the constancy in the canonical fusion peptide sequences of mosquito-borne, tick-borne and viruses with no known vector to include more recently-sequenced viruses. The mosquito-borne signature amino acid, G104, was also found in flaviviruses with no known vector and with the cell-fusion related viruses. Despite the constan