Fusion glycoprotein

The potential complications of inferring phylogeny from molecular data have also been emphasized by studies of Ebola virus. One protein, the fusion glycoprotein gp2, showed structural homology to viruses that were quite unrelated (Malashkevich et al, 1999 Weissenhorn et al, 1998), whereas another, the matrix protein, showed no homology even to its closest relatives (Dessen et al, 2000). 

Lescar, J., Roussel, A., Wein, M. W., Navaza, J., Fuller, S. D., Wengler, G., Wengler, G., and Rey, F. A. (2001). The fusion glycoprotein shell of Semliki Forest virus An icosahedral assembly primed for fusogenic activation at endosomal pH. Cell 105, 137-148. 

Feldman SA, Audet S, Beeler JA (2000) The fusion glycoprotein of human respiratory syncytial virus facilitates virus attachment and infectivity via an interaction with cellular heparan sulfate. J Virol 74 6442-6447... 

Ghildyal R, Hardey C, Varrasso A et al. Surfactant protein A binds to the fusion glycoprotein of respiratory syncytial virus and neutralizes virion infectivity. J Infect Dis 1999 180(6) 2009-13. 

Rosenthal PB, Zhang X, Formanowski F, Fitz W, Wong CH, Meier-Ewert H, Skehel JJ, Wiley DC (1998) Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C... 

Other human viral pathogens toward which castanospermine (654) displayed activity include NSW-N8 strain of influenza A virus" and type 3 parainfluenza virus.It also delayed the association of measles virus fusion glycoproteins with calnexin, and reduced the production of the virus particles in human epidermoid carcinoma cells. °... 

Rosenthal, P.B., Zang, X., Formanowski, F., Fitz, W., Wong, C.-H., Meier-Ewert, H., Skehel, J.J., and Wiley, D.C. Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza... 

Daniels, R.S., et al. Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell 40 431-439, 1985. 

Many enveloped viruses share a common mechanism of fusion, mediated by a virus-encoded glycoprotein that contains heptad repeats in its extraceUnlar domain. Dnring the fnsion process, these domains rearrange to form highly structured and thermodynamically stable coiled-coils. Viruses encoding fusion proteins that have these domains inclnde members of the paramyxovirus family (e.g., respiratory syncytial virus, metapneumovirus, and measles virus), ebola virus, influenza, and members of the retroviridae (e.g., human T cell lenkemia virus type-1 and human immunodeficiency virus type-1, HlV-1). Peptide inhibitors of fusion that disrupt the... 

He Y, Vassell R, Zaitseva M, Nguyen N, Yang Z, Weng Y, Weiss CD (2003) Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites. J Virol 77 1666-1671... 

Jiang S, Lin K, Strick N, Neurath AR (1993) Inhibition of HIV-1 infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein GP41. Biochem Biophys Res Commun 195 533-538... 

After the virus has attached to CD4 and chemokine receptors, another viral glycoprotein (gp41) assists with viral fusion to the cell and internalization of the viral contents. The viral contents include single-stranded RNA, an RNA-dependent DNA polymerase (also known as reverse transcriptase), and other enzymes. Using the single-stranded viral RNA as a template, reverse transcriptase synthesizes a complementary strand of DNA. The single-stranded viral RNA is removed from the newly formed DNA strand by ribonuclease H, and reverse transcriptase completes the synthesis of double-stranded DNA. The... 

Wyss S, Dimitrov AS, Baribaud F, Edwards TG, Blumenthal R, Hoxie JA. Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain in the gp41 cytoplasmic tail. J Virol 2005 79(19) 12231-12241. 

Infection of CD4+ cells commences via interaction between gp 120 and the CD4 glycoprotein, which effectively acts as the viral receptor. Entry of the virus into the cell, which appears to require some additional cellular components, occurs via endocytosis and/or fusion of the viral and cellular membranes. The gp 41 transmembrane protein plays an essential role in this process. 

Figure 7. A recently proposed HIV adsorption/fusion mechanism onto T cel I s CD4 receptor with coreceptor (chemokine, etc.), fol lowed by breaching the T-cell membrane by HIV glycoprotein gp41.

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