title: The 19-27 amino acid segment of gp51 adopts an amphiphilic structure and plays a key role in the fusion events induced by bovine leukemia virus.
abstract: Previous results indicate that the external glycoprotein gp51 of bovine leukemia virus plays an important role in the process of cell fusion induced by bovine leukemia virus (Bruck, C., Mathot, S., Portetelle, D., Berte, C., Franssen, J. D., Herion, P., and Burny, A. (1982) Virology 122, 342-352; Vonèche, V., Portetelle., D., Kettmann, R., Willems, L., Limbach, K., Paoletti, E., Ruysschaert, J. M., Burny, A., and Brasseur, R. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 3810-3814) and suggest that a region encompassing residues 23 and 25 of gp51 is involved in this process (Portetelle, D., Couez, D., Bruck, C., Kettmann, R., Mammerickx, M., Van der Maaten, M., Brasseur, R., and Burny, A. (1989) Virology 169, 27-33; Mamoun, R., Morisson, M., Rebeyrotte, N., Busetta, B., Couez, D., Kettmann, R., Hospital, M., and Guillemain, B. (1990) J. Virol. 64, 4180-4188). X-ray diffraction studies performed on envelope glycoproteins of influenza virus indicate that the NH2-terminal part of the external glycoprotein lies very close to the fusion peptide. The same overall structure seems to exist in human immunodeficiency virus as suggested by site-directed mutagenesis followed by syncytia induction assays. Our theoretical studies indicate that a segment expanding between residues 19 and 27 of gp51 probably adopts an amphipathic beta-strand structure. We hypothesize that the amphipathic 19-27 structure of gp51 plays an important role in the process of membrane fusion by interacting with the fusion peptide or with another region of gp30. Mutational analysis disrupting the amphipathy of the 19-27 region strongly altered the fusogenic capacity of the gp51-gp30 complex.
authors.affiliation: Laboratory of Molecular Biology and Animal Physiology, Faculty of Agronomy, Gembloux, Belgium.
authors.forename: V
authors.initials: V
authors.lastname: Vonèche
authors.forename: I
authors.initials: I
authors.lastname: Callebaut
authors.forename: R
authors.initials: R
authors.lastname: Kettmann
authors.forename: R
authors.initials: R
authors.lastname: Brasseur
authors.forename: A
authors.initials: A
authors.lastname: Burny
authors.forename: D
authors.initials: D
authors.lastname: Portetelle
mesh_terms: D000595:Amino Acid Sequence; D015153:Blotting, Western; D002459:Cell Fusion; D004797:Enzyme-Linked Immunosorbent Assay; D005455:Fluorescent Antibody Technique; D001909:Leukemia Virus, Bovine / Q000502:physiology*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010446:Peptide Fragments / Q000502:physiology*; D014759:Viral Envelope Proteins / Q000502:physiology*; D014961:X-Ray Diffraction
chemical_list: D010446:Peptide Fragments; D014759:Viral Envelope Proteins