Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus

Gallaher, William R.

doi:10.1016/0092-8674(87)90485-5

Cited by 425 publications

(262 citation statements)

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“…This is similar to that found for HIV where gpl20 is believed to be involved in steps leading to fusion (Ratner, 1992). In HIV, the hydrophobic domain in the Nterminal part of the transmembrane protein gp41 is active in fusion (Gallaher, 1987). The pl5E has a similar hydrophobic domain (amino acids 5 to 24 in pl5E of Mo-MLV).…”

Section: Introductionsupporting

confidence: 60%

Mutational analysis of Moloney murine leukaemia virus surface protein gp70

Skov

Andersen

1993

Journal of General Virology

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Ten mutations were generated in the env gene of Moloney murine leukaemia virus DNA. The mutations were made by site-directed mutagenesis to alter basic amino acids (lysine or arginine) in the surface glycoprotein gp70. Mutants were investigated following transfection into NIH/3T3 cells. All 10 mutants released virion particles into the medium, suggesting that none of the mutations affected overall viral gene expression or virion budding. Two mutants were positive in XC plaque assay, reverse transcriptase assay and re-infection experiments, showing that these mutations occurred in parts of the molecule not essential for infection. Three mutants were negative in both the XC plaque assay and re-infection experiments, suggesting that they make noninfectious virus particles. The results indicate a defect in the early phase of infection, perhaps in receptor binding or in the fusion ofvirion and host membranes. The other mutations resulted in reduced infectivity of released virion particles.

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Section: Introductionsupporting

confidence: 60%

Mutational analysis of Moloney murine leukaemia virus surface protein gp70

Skov

Andersen

1993

Journal of General Virology

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“…This moderately hydrophobic sequence contains the tetrapeptide G-L-F-G which is also found at the fusion-active amino terminus of the influenza virus HA2 (Wharton, 1987). A similar sequence is also found in the fusion proteins of paramyxo-and retroviruses (Gallaher, 1987). One might therefore speculate that this sequence contributes to the fusion activity of flaviviruses after acid pH-induced conformational changes (Roehrig et al, 1989).…”

Section: Discussionmentioning

confidence: 80%

“…In the case of myxo-, paramyxo-and retroviruses, a highly conserved hydrophobic sequence is liberated at or near the amino terminus of the membrane-associated part of the cleaved proteins (Bosch et al, 1989;Gallaher, 1987;Morrison, 1988;Wharton, 1987). Depending on the virus, this structural element is thought to trigger fusion activity either at physiological pH or after acid pH-induced conformational changes of the protein (Marsh & Helenius, 1989).…”

Section: Discussionmentioning

confidence: 99%

Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions

Guirakhoo

Heinz²,

Mandl³

et al. 1991

Journal of General Virology

170

156

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The fusion activity of flaviviruses [tick-borne encephalitis (TBE) virus and Japanese encephalitis virus] was assessed by inducing fusion from without of C6/36 mosquito cells with purified virus preparations. Membrane fusion and polykaryocyte formation was observed only after incubating the viruses at acidic pH. Two groups of monoclonal antibodies reacting with distinct non-overlapping antigenic domains on the TBE virus protein E inhibited fusion from without. One of these domains contains the most highly conserved and putative fusion-active sequence of the flavivirus protein E. Of five TBE virus monoclonal antibody escape mutants, each defined by a single amino acid substitution in the envelope protein E, one revealed a reduced fusion activity and another one a lower pH threshold. TBE virus grown in the presence of ammonium chloride as well as Langat virus purified from the supernatant of infected chick embryo cells contained the precursor of protein M (prM) rather than M itself. These 'immature' virions did not cause fusion from without, suggesting that the proteolytic processing of prM may be necessary for the generation of fusion-competent virions.

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“…Amino acid homology between fusion proteins of different viruses is usually of less than 20%. In contrast FP homology for the same proteins can be as high as 90% [52]. FPs are also unusually enriched in Ala and Gly residues [53].…”

Section: Ii: Hiv-1 Fusion Inhibition By Targeting the Fusion Peptidementioning

confidence: 99%

Membrane-Transferring Regions of gp41 as Targets for HIV-1 Fusion Inhibition and Viral Neutralization

Huarte

Lorizate²,

Pérez‐Payá³

et al. 2011

CTMC

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Abstract:The fusogenic function of HIV-1 gp41 transmembrane Env subunit relies on two different kinds of structural elements: i) a collapsible ectodomain structure (the hairpin or six-helix bundle) that opens and closes, and ii) two membrane-transferring regions (MTRs), the fusion peptide (FP) and the membrane-proximal external region (MPER), which ensure coupling of hairpin closure to apposition and fusion of cell and viral membranes. The isolation of naturally produced short peptides and neutralizing IgG-s, that interact with FP and MPER, respectively, and block viral infection, suggests that these conserved regions might represent useful targets for clinical intervention.Furthermore, MTR-derived peptides have been shown to be membrane-active. Here, it is discussed the potential use of these molecules and how the analysis of their membrane activity in vitro could contribute to the development of HIV fusion inhibitors and effective immunogens.2

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Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus

Cited by 425 publications

References 0 publications

Mutational analysis of Moloney murine leukaemia virus surface protein gp70

Mutational analysis of Moloney murine leukaemia virus surface protein gp70

Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions

Membrane-Transferring Regions of gp41 as Targets for HIV-1 Fusion Inhibition and Viral Neutralization

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