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Proc Natl Acad Sci U S A. May 1, 1992; 89(9): 3810–3814.
PMCID: PMC525580

Fusogenic segments of bovine leukemia virus and simian immunodeficiency virus are interchangeable and mediate fusion by means of oblique insertion in the lipid bilayer of their target cells.


Modified bovine leukemia virus (BLV) glycoproteins were expressed by using vaccinia virus recombinants, and their fusogenic capacities were examined by a syncytia-formation assay. This analysis indicates that (i) both BLV envelope glycoproteins gp51 and gp30 are necessary for cell fusion; (ii) insertion of the N-terminal segment of gp30 (fusion peptide) into the lipid bilayer in an oblique orientation, as predicted by computer conformational analysis, results in fusogenic capacities higher than insertion in a perpendicular or parallel orientation; and (iii) replacement of the BLV fusion peptide with its simian immunodeficiency virus counterpart does not modify the fusogenic capacity of the BLV glycoprotein.

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Selected References

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  • Kowalski M, Potz J, Basiripour L, Dorfman T, Goh WC, Terwilliger E, Dayton A, Rosen C, Haseltine W, Sodroski J. Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1. Science. 1987 Sep 11;237(4820):1351–1355. [PubMed]
  • Bosch ML, Earl PL, Fargnoli K, Picciafuoco S, Giombini F, Wong-Staal F, Franchini G. Identification of the fusion peptide of primate immunodeficiency viruses. Science. 1989 May 12;244(4905):694–697. [PubMed]
  • Freed EO, Myers DJ, Risser R. Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proc Natl Acad Sci U S A. 1990 Jun;87(12):4650–4654. [PMC free article] [PubMed]
  • Brasseur R, Cornet B, Burny A, Vandenbranden M, Ruysschaert JM. Mode of insertion into a lipid membrane of the N-terminal HIV gp41 peptide segment. AIDS Res Hum Retroviruses. 1988 Apr;4(2):83–90. [PubMed]
  • Brasseur R, Lorge P, Goormaghtigh E, Ruysschaert JM, Espion D, Burny A. The mode of insertion of the paramyxovirus F1 N-terminus into lipid matrix, an initial step in host cell/virus fusion. Virus Genes. 1988 Jul;1(4):325–332. [PubMed]
  • Brasseur R, Vandenbranden M, Cornet B, Burny A, Ruysschaert JM. Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins. Biochim Biophys Acta. 1990 Nov 16;1029(2):267–273. [PubMed]
  • Burny A, Cleuter Y, Kettmann R, Mammerickx M, Marbaix G, Portetelle D, Van den Broeke A, Willems L, Thomas R. Bovine leukemia: facts and hypotheses derived from the study of an infectious cancer. Adv Vet Sci Comp Med. 1988;32:149–170. [PubMed]
  • Graves DC, Jones LV. Early syncytium formation by bovine leukemia virus. J Virol. 1981 Jun;38(3):1055–1063. [PMC free article] [PubMed]
  • Bruck C, Mathot S, Portetelle D, Berte C, Franssen JD, Herion P, Burny A. Monoclonal antibodies define eight independent antigenic regions on the bovine leukemia virus (BLV) envelope glycoprotein gp51. Virology. 1982 Oct 30;122(2):342–352. [PubMed]
  • Willems L, Bruck C, Portetelle D, Burny A, Kettmann R. Expression of a cDNA clone corresponding to the long open reading frame (XBL-I) of the bovine leukemia virus. Virology. 1987 Sep;160(1):55–59. [PubMed]
  • Taylor JW, Ott J, Eckstein F. The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA. Nucleic Acids Res. 1985 Dec 20;13(24):8765–8785. [PMC free article] [PubMed]
  • Sayers JR, Schmidt W, Eckstein F. 5'-3' exonucleases in phosphorothioate-based oligonucleotide-directed mutagenesis. Nucleic Acids Res. 1988 Feb 11;16(3):791–802. [PMC free article] [PubMed]
  • Mackett M, Smith GL, Moss B. General method for production and selection of infectious vaccinia virus recombinants expressing foreign genes. J Virol. 1984 Mar;49(3):857–864. [PMC free article] [PubMed]
  • Chakrabarti S, Brechling K, Moss B. Vaccinia virus expression vector: coexpression of beta-galactosidase provides visual screening of recombinant virus plaques. Mol Cell Biol. 1985 Dec;5(12):3403–3409. [PMC free article] [PubMed]
  • Portetelle D, Limbach K, Burny A, Mammerickx M, Desmettre P, Riviere M, Zavada J, Paoletti E. Recombinant vaccinia virus expression of the bovine leukaemia virus envelope gene and protection of immunized sheep against infection. Vaccine. 1991 Mar;9(3):194–200. [PubMed]
  • Portetelle D, Mammerickx M, Burny A. Use of two monoclonal antibodies in an ELISA test for the detection of antibodies to bovine leukaemia virus envelope protein gp51. J Virol Methods. 1989 Feb;23(2):211–222. [PubMed]
  • Portetelle D, Couez D, Bruck C, Kettmann R, Mammerickx M, Van der Maaten M, Brasseur R, Burny A. Antigenic variants of bovine leukemia virus (BLV) are defined by amino acid substitutions in the NH2 part of the envelope glycoprotein gp51. Virology. 1989 Mar;169(1):27–33. [PubMed]
  • Brasseur R, Goormaghtigh E, Ruysschaert JM. Theoretical conformational analysis of phospholipids bilayers. Biochem Biophys Res Commun. 1981 Nov 16;103(1):301–310. [PubMed]
  • Brasseur R. Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations. J Biol Chem. 1991 Aug 25;266(24):16120–16127. [PubMed]
  • Brasseur R, Ruysschaert JM. Conformation and mode of organization of amphiphilic membrane components: a conformational analysis. Biochem J. 1986 Aug 15;238(1):1–11. [PMC free article] [PubMed]
  • Eisenberg D, Weiss RM, Terwilliger TC. The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature. 1982 Sep 23;299(5881):371–374. [PubMed]
  • Eisenberg D, Schwarz E, Komaromy M, Wall R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol. 1984 Oct 15;179(1):125–142. [PubMed]
  • Gething MJ, Doms RW, York D, White J. Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus. J Cell Biol. 1986 Jan;102(1):11–23. [PMC free article] [PubMed]
  • Gallaher WR. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell. 1987 Jul 31;50(3):327–328. [PubMed]
  • McCune JM, Rabin LB, Feinberg MB, Lieberman M, Kosek JC, Reyes GR, Weissman IL. Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell. 1988 Apr 8;53(1):55–67. [PubMed]
  • Harter C, James P, Bächi T, Semenza G, Brunner J. Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide". J Biol Chem. 1989 Apr 15;264(11):6459–6464. [PubMed]
  • Martin I, Defrise-Quertain F, Mandieau V, Nielsen NM, Saermark T, Burny A, Brasseur R, Ruysschaert JM, Vandenbranden M. Fusogenic activity of SIV (simian immunodeficiency virus) peptides located in the GP32 NH2 terminal domain. Biochem Biophys Res Commun. 1991 Mar 29;175(3):872–879. [PubMed]
  • Horth M, Lambrecht B, Khim MC, Bex F, Thiriart C, Ruysschaert JM, Burny A, Brasseur R. Theoretical and functional analysis of the SIV fusion peptide. EMBO J. 1991 Oct;10(10):2747–2755. [PMC free article] [PubMed]

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