Antibody-mediated inhibition of filovirus budding

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Monoclonal antibodies (MAbs) specific to Marburg virus glycoprotein (GP) were produced to analyze their activity to suppress the virus budding. We found that some of the MAbs, which did not have a classical neutralizing activity, efficiently inhibited the budding and release of MARV particles from infected cells. A couple of escape variants selected by these MAbs had deletions of the mucin-like region in GP or single amino acid substitutions in the furin-recognition motif in GP. These results demonstrate a novel mechanism of antibody-mediated inhibition of MARV budding and the extraordinary structural flexibility and variability of MARV GP to escape from immunological pressure of antibodies.