1999
DOI: 10.1080/096876899294706
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Structural basis for membrane fusion by enveloped viruses

Abstract: Enveloped viruses such as HIV-1, influenza virus, and Ebola virus express a surface glycoprotein that mediates both cell attachment and fusion of viral and cellular membranes. The membrane fusion process leads to the release of viral proteins and the RNA genome into the host cell, initiating an infectious cycle. This review focuses on the HIV-1 gp41 membrane fusion protein and discusses the structural similarities of viral membrane fusion proteins from diverse families such as Retroviridae (HIV-1), Orthomyxovi… Show more

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Cited by 363 publications
(348 citation statements)
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“…A conformational change in the gp41/gp120 oligomer allows the fusion peptide sequence, located on the N terminus of gp41, to insert into the membrane of the target cell (3). The gp41 ectodomain is then thought to undergo a series of conformational changes to form the fusion-active state, which is believed to bring the viral and cellular membranes into closer proximity to facilitate membrane fusion (2,3). Crystallographic studies provide support for a model where gp41 adopts a six-helix bundle structure late in the fusion process (4)(5)(6), and this structure is likely involved in the final steps before fusion.…”
mentioning
confidence: 87%
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“…A conformational change in the gp41/gp120 oligomer allows the fusion peptide sequence, located on the N terminus of gp41, to insert into the membrane of the target cell (3). The gp41 ectodomain is then thought to undergo a series of conformational changes to form the fusion-active state, which is believed to bring the viral and cellular membranes into closer proximity to facilitate membrane fusion (2,3). Crystallographic studies provide support for a model where gp41 adopts a six-helix bundle structure late in the fusion process (4)(5)(6), and this structure is likely involved in the final steps before fusion.…”
mentioning
confidence: 87%
“…H IV type 1 (HIV-1) fusion is mediated by a complex set of interactions involving cellular receptors and viral glycoproteins (1,2). The precise nature of these interactions remains unclear, but in the current model, viral attachment occurs via an interaction between gp120 and CD4, along with chemokine receptors (such as CCR5 or CXCR4) that act as viral coreceptors for HIV-1.…”
mentioning
confidence: 99%
“…This general architecture is observed in other viral fusion proteins, such as other retroviruses Fass and Kim, 1995;Lu et al, 1995;Fass et al, 1996;Malashkevich et al, 1998), Ebola GP (Wiessenhorn et al., 1998Malashkevich et al, 1999), paramyxovirus F (Joshi et al, 1998Baker et al, 1999;Dutch et al, 1999), and influenza hemagglutinin (HA) proteins (Carr and Kim, 1993;Bullough et al, 1994). Conversion of fusion proteins to a rod-like structure via formation of a long trimeric coiled coil upon low pH application has been observed and forms the basis of a proposed spring-loaded mechanism by which hydrophobic amino-terminal "fusion peptides" are projected into the target membrane, ultimately resulting in fusion of the viral envelope with the target cell membrane (Carr and Kim 1993;Chan et al, 1997;Weissenhorn et al, 1997Weissenhorn et al, , 1999.For paramyxoviruses and HIV, evidence suggests that the hydrophobic 4-3 heptad repeats are directly involved in the viral fusion process. Single leucine-to-alanine mutations of the F proteins from paramyxoviruses do not block fusion, but multiple leucine-to-alanine mutations do abolish fusion activity of the protein but do not negatively affect F protein oligomerization or cell surface expression (Buckland et al, 1992;Sergel-Germano et al, 1994;Reitter et al, 1995).…”
mentioning
confidence: 99%
“…Although the understanding of enveloped-virus entry via membrane fusion has seen many advances (1)(2)(3), the entry mechanisms of nonenveloped animal viruses remain elusive. Mammalian orthoreovirus (reovirus) is a large nonenveloped virus with a 10-segmented dsRNA genome.…”
mentioning
confidence: 99%