A CD46CD[55–46] chimeric receptor, eight short consensus repeats long, acts as an inhibitor of both CD46 (MCP)- and CD150 (SLAM)-mediated cell–cell fusion induced by CD46-using measles virus
Autor: | Plemper, R., Hammond, A., Fielding, A., Cattaneo, R., Lanteri, Marc, Gerlier, D., De Sousa, Emmanuel, Christiansen, Dale, Kyriakou, Peter, Loveland, Bruce, Wild, Fabian |
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Přispěvatelé: | AstraZeneca, Virologie et pathogenèse virale (VPV), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Immunite et Vaccination, Institut National de la Santé et de la Recherche Médicale (INSERM) |
Jazyk: | angličtina |
Rok vydání: | 2002 |
Předmět: |
Repetitive Sequences
Amino Acid viruses Recombinant Fusion Proteins Molecular Sequence Data Immunoglobulins Receptors Cell Surface CHO Cells Biology Membrane Fusion Cell membrane Measles virus Membrane Cofactor Protein Signaling Lymphocytic Activation Molecule Family Member 1 Antigens CD Virology Cricetinae medicine Animals Amino Acid Sequence Binding site Receptor ComputingMilieux_MISCELLANEOUS Glycoproteins Membrane Glycoproteins CD46 biology.organism_classification female genital diseases and pregnancy complications Transmembrane protein medicine.anatomical_structure Viral replication Cytoplasm [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology |
Zdroj: | Journal of General Virology Journal of General Virology, Microbiology Society, 2002, 83 (5), pp.1147-1155. ⟨10.1099/0022-1317-83-5-1147⟩ |
ISSN: | 0022-1317 1465-2099 |
DOI: | 10.1099/0022-1317-83-5-1147⟩ |
Popis: | According to their cellular receptor use, measles virus (MV) strains can be separated into two phenotypes, CD46-using and CD46-non-using. A long chimeric receptor, CD46CD[55–46], was generated from the CD46 backbone, encompassing the four short consensus repeat (SCR) domains of CD46 linked via a flexible glycine hinge to SCR1 and SCR2 of CD55, SCR3 and SCR4 of CD46 and the STP, transmembrane and cytoplasmic tail of CD46. This chimeric receptor was proficient for MV binding but deficient in mediating MV-induced cell-to-cell fusion and virus replication, possibly due to the extended distance between the MV haemagglutinin (H) binding site (CD46 SCR1–SCR2) and the cell membrane. When coexpressed with either wild-type CD46 or CD150, this fusion-incompetent receptor exerted a dominant negative effect and inhibited both cell-to-cell fusion and entry of MV with CD46-using, but not CD46-non-using, phenotype. A soluble octameric CD46–C4bpα exhibited similar CD46- and CD150-mediated fusion inhibition properties only against CD46-using MV. This suggests that the long CD46CD[55–46] receptor acts by sequestering incoming MV prior to its binding to the shorter functional CD46 or CD150 receptor. |
Databáze: | OpenAIRE |
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