Mutations in the p53 tumor-suppressor gene are frequently associated with bovine leukemia virus-induced leukemogenesis in cattle but not in sheep.

in Virology (1995), 209(2),

TaqI restriction fragment length polymorphism for pig growth hormone in pigs

in 14th International Pig Veterinary Society Congress (1995)

Nucleotide sequence of the bovine P53 tumor-suppressor cDNA.

in DNA Sequence : The Journal of DNA Sequencing & Mapping (1995), 5(4),

Cloning And Characterization Of Mn, A Human Tumor-Associated Protein With A Domain Homologous To Carbonic-Anhydrase And A Putative Helix-Loop-Helix Dna-Binding Segment

in Oncogene (1994), 9(10),

Involvement Of The Cyclic Amp-Responsive Element-Binding Protein In Bovine Leukemia-Virus Expression In-Vivo

in Journal of Virology (1994), 68(9),

Expression Of Interleukin-6 Receptors And Interleukin-6 Messenger-Rna By Bovine Leukemia Virus-Induced Tumor-Cells

in Cytokine (1994), 6(6),

Bovine Leukemia Virus

in The Retroviridae (1994)

Bovine leukemia virus, an animal model for the study of intrastrain variability.

in Journal of Virology (1993), 67(2),

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

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 ▲]

The interaction between Bovine Leukemia Virus and its target cell.

in AIDS Research and Human Retroviruses (1992), 8

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 ▲]