Murine Anti-vaccinia Virus D8 Antibodies Target Different Epitopes and Differ in Their Ability to Block D8 Binding to CS-E

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Vaccinia virus (VACV) is an orthopox virus and considered the gold standard of vaccines as it was used to eradicate smallpox from the human population. Inoculation with VACV leads to a strong B cell immune response and the production of potent antibodies that simultaneously target several envelope proteins of the virus. Among those viral proteins, D8 is an adhesion molecule that binds chondroitin sulfate, a glycosaminoglycan, on the host cell surface. Here, we identified chondroitin sulfate E (CS-E), as the preferred ligand for D8 and assessed the role of a panel of anti-D8 antibodies in preventing D8 binding to CS-E. We further mapped the binding site of each antibody on the D8 surface to reveal the targeted epitopes. Finally, using several truncated D8 constructs, we identified that the C-terminal domain of D8 that is not involved in CS-E binding is in fact involved in oligomerization of native D8 in vitro and likely, also on the virion, as a means of increasing binding affinity to increase viral adhesion to CS on the host cell.

Vyšlo v časopise: Murine Anti-vaccinia Virus D8 Antibodies Target Different Epitopes and Differ in Their Ability to Block D8 Binding to CS-E. PLoS Pathog 10(12): e32767. doi:10.1371/journal.ppat.1004495
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004495

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