Cloning and expression of the complement receptor glycoprotein C from Herpesvirus simiae (herpes B virus): protection from complement-mediated cell lysis
| Autor: | L. Harrington, Dietrich Falke, Christian Wechselberger, Alice M. Bennett, Hartwig P. Huemer |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Cytotoxicity
Immunologic Herpes B virus viruses Complement Pathway Alternative Molecular Sequence Data Herpesvirus 1 Cercopithecine Complement receptor Biology Transfection medicine.disease_cause Virus Cell Line Viral Envelope Proteins Virology medicine Animals Humans Amino Acid Sequence Cloning Molecular Peptide sequence Sequence Analysis DNA biology.organism_classification Complement system Herpes simplex virus Cell culture Complement C3b Receptors Complement 3b Alternative complement pathway |
| Zdroj: | Journal of General Virology. 84:1091-1100 |
| ISSN: | 1465-2099 0022-1317 |
| DOI: | 10.1099/vir.0.18949-0 |
| Popis: | Simian herpes B virus (SHBV) is the herpes simplex virus (HSV) homologue for the species MACACA: Unlike in its natural host, and unlike other animal herpesviruses, SHBV causes high mortality in accidentally infected humans. SHBV-infected cells, like those infected with HSV-1 and equine herpesvirus types 1 and 4, express complement C3 receptor activity. To study immunoregulatory functions involved in susceptibility/resistance against interspecies transmission, the SHBV glycoprotein C (gC(SHBV)) gene (encoding 467 aa) was isolated. Sequence analysis revealed amino acid identity with gC proteins from HSV-2 (46.9 %), HSV-1 (44.5 %) and pseudorabies virus (21.2 %). Highly conserved cysteine residues were also noted. Similar to gC(HSV-2), gC(SHBV) is less glycosylated than gC(HSV-1), resulting in a molecular mass of 65 kDa if expressed in replication-deficient vaccinia virus Ankara. Stable transfectants expressing full-length gC(SHBV) on the cell surface induced C3 receptor activity and were substantially protected from complement-mediated lysis; no protection was observed with control constructs. This suggests that expression of the gC homologues on infected cell surfaces might also contribute to the survival of infected cells in addition to decreased virion inactivation. Interestingly, soluble gC(SHBV) isolated from protein-free culture supernatants did not interfere with the binding of the alternative complement pathway activator properdin to C3b, which is similar to our findings with gC(HSV-2) and could be attributed to major differences in the amino-terminal portion of the protein with extended deletions in both gC(SHBV) and gC(HSV-2). Binding of recombinant gC(SHBV) to polysulphates was observed. This, together with the heparin-sensitivity of the gC(SHBV)-C3 interaction on the infected cell surface, suggests a role in adherence to heparan sulphate, similar to the gC proteins of other herpesviruses. |
| Databáze: | OpenAIRE |
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