Differential stability and fusion activity of Lyssavirus glycoprotein trimers
| Autor: | Pierre Perrin, Antoine P. Maillard, Yves Gaudin, Emmanuel Desmezieres, Noël Tordo |
|---|---|
| Přispěvatelé: | Inconnu, Virologie moléculaire et structurale (VMS), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Lyssavirus, Institut Pasteur [Paris] (IP), This work was supported by CNRS (UMR 2472) and by funds from the ‘ACI Blanche’., Institut Pasteur [Paris] |
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Cancer Research
MESH: Hydrogen-Ion Concentration MESH: Lyssavirus [SDV]Life Sciences [q-bio] MESH: Cricetinae Trimer medicine.disease_cause Membrane Fusion Cell Fusion Viral Envelope Proteins Chaps Cricetinae MESH: Animals Antigens Viral chemistry.chemical_classification 0303 health sciences Cell fusion biology Hydrogen-Ion Concentration 3. Good health MESH: Rabies virus Infectious Diseases MESH: Antigens Viral Dimerization Rabies Recombinant Fusion Proteins MESH: Glycoproteins Mokola virus Transfection MESH: Membrane Fusion Virus Cell Line 03 medical and health sciences Virology medicine MESH: Recombinant Fusion Proteins Animals Fusion Lyssavirus 030304 developmental biology Glycoproteins 030306 microbiology MESH: Transfection Rabies virus biology.organism_classification Molecular biology Mokola MESH: Cell Line chemistry MESH: Dimerization MESH: Viral Envelope Proteins MESH: Cell Fusion Glycoprotein |
| Zdroj: | Virus Research Virus Research, Elsevier, 2003, 91 (2), pp.181-187 Virus Research, 2003, 91 (2), pp.181-187. ⟨10.1016/s0168-1702(02)00267-8⟩ Virus Research, Elsevier, 2003, 91 (2), pp.181-187. ⟨10.1016/s0168-1702(02)00267-8⟩ |
| ISSN: | 0168-1702 |
| Popis: | International audience; The oligomeric structure and the fusion activity of lyssavirus glycoprotein (G) was studied by comparing G from Mokola virus (GMok) and rabies virus (PV strain) (GPV), which are highly divergent lyssaviruses. G expressed at the surface of BSR cells upon either plasmid transfection or virus infection are shown to be mainly trimeric after cross-linking experiments. However, solubilization by a detergent (CHAPS) and analysis in sucrose sedimentation gradient evidenced that GMok trimer is less stable than GPV trimer. A chimeric glycoprotein (G Mok-PV) associating the N-terminal half of GMok to the C-terminal half part of GPV formed trimers with an intermediate stability, indicating that the G C-terminal domain is essential in trimer stability. A cell to cell fusion assay revealed that GMok (and not G Mok-PV) was able to induce fusion at a higher pH (0.5 pH unit) than GPV. Such differences in the oligomeric structure stability and in the fusion activity of lyssavirus glycoproteins may partly account for the previously reported differences of their immunogenic and pathogenic properties. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect