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See detailEnhancement of bovine leukemia virus-induced syncytia formation by di- and tripeptides.
Voneche, V.; Callebaut, I.; Lambrecht, B. et al

in Virology (1993), 192(1),

Short hydrophobic peptides were previously shown to inhibit infectivity of para- and orthomyxoviruses. We tested the ability of a series of di- and tripeptides to interfere with cell fusion induced by ... [more ▼]

Short hydrophobic peptides were previously shown to inhibit infectivity of para- and orthomyxoviruses. We tested the ability of a series of di- and tripeptides to interfere with cell fusion induced by bovine leukemia virus (BLV). Peptides containing a hydrophobic contribution and/or a positive net charge strongly enhanced syncytia formation induced by BLV on CC81 indicator cells. The size of the multinucleated cells was strongly increased (up to 10-fold) in the presence of the enhancer peptides whereas no effect was observed on the indicator cells in the absence of BLV. The peptides thus amplified the fusion process initiated by BLV envelope glycoproteins. The effect was dose-dependent at concentrations ranging from 20 to 640 microM and did not result from an increased expression of BLV proteins. The peptides did not compete with anti-gp51 monoclonal antibodies for the recognition of eight well-defined epitopes of gp51. We consequently hypothesize that the enhancer peptides interact with the membrane of BLV-producing cells and/or indicator cells and propose a model based on molecular modeling. [less ▲]

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See detailIn vivo infection of sheep by bovine leukemia virus mutants.
Willems, Luc ULg; Kettmann, Richard ULg; Dequiedt, Franck ULg et al

in Journal of virology (1993), 67(7),

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See detailMapping Of B-Neutralizing And T-Helper Cell Epitopes On The Bovine Leukemia-Virus External Glycoprotein Gp51
Callebaut, I.; Voneche, V.; Mager, A. et al

in Journal of Virology (1993), 67(9),

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See detailFusogenic 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
Voneche, V.; Portetelle, Daniel ULg; Kettmann, Richard ULg et al

in Proceedings of the National Academy of Sciences of the United States of America (1992), 89(9),

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 ... [more ▼]

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. [less ▲]

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See detailThe 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
Voneche, V.; Callebaut, I.; Kettmann, Richard ULg et al

in Journal of Biological Chemistry (1992), 267(21),

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 ... [more ▼]

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; Voneche, 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. [less ▲]

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