Expression of the recombinant anchorless N-terminal domain of mouse hepatitis virus (MHV) receptor makes hamster of human cells susceptible to MHV infection
| Autor: | S Gagneten, Gabriela S. Dveksler, Kathryn V. Holmes, Christine B. Cardellichio, Charles A. Scanga |
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| Rok vydání: | 1996 |
| Předmět: |
viruses
Molecular Sequence Data Immunology Hamster Transfection Microbiology law.invention Mice Mouse hepatitis virus law Cricetinae Virology Animals Humans Amino Acid Sequence chemistry.chemical_classification Murine hepatitis virus biology Virus receptor virus diseases biology.organism_classification Molecular biology Recombinant Proteins Transmembrane domain chemistry Insect Science biology.protein Recombinant DNA Receptors Virus Antibody Glycoprotein Research Article |
| Zdroj: | Journal of Virology. 70:4142-4145 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.70.6.4142-4145.1996 |
| Popis: | Mouse hepatitis virus (MHV) receptor, the receptor for the murine coronavirus MHV, was expressed in MHV-resistant hamster and human cells as a series of mutant, recombinant glycoproteins with carboxy-terminal deletions lacking the cytoplasmic tail, transmembrane domain, and various amounts of the immunoglobulin constant-region-like domains. The soluble receptor glycoproteins containing the N-terminal virus-binding domain were released into the supernatant medium and inactivated the infectivity of MHV-A59 virions in a concentration-dependent manner. Surprisingly, some of the anchorless glycoproteins were found on the plasma membranes of transfected cells by flow cytometry, and these cells were rendered susceptible to infection with three strains of MHV. Thus, in the cells in which the anchorless, recombinant receptor glycoprotein is synthesized, some of the protein is bound to an unidentified moiety on the plasma membrane, which allows it to serve as a functional virus receptor. |
| Databáze: | OpenAIRE |
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