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Abstract

Orthobunyaviruses are enveloped viruses that are arthropod-transmitted and cause disease in humans and livestock. Viral attachment and entry are mediated by the envelope glycoproteins Gn and Gc, and the major glycoprotein, Gc, of certain orthobunyaviruses is targeted by neutralizing antibodies. The domains in which the epitopes of such antibodies are located on the glycoproteins of the animal orthobunyavirus Schmallenberg virus (SBV) have not been identified. Here, we analysed the reactivity of a set of mAbs and antisera against recombinant SBV glycoproteins. The M-segment-encoded proteins Gn and Gc of SBV were expressed as full-length proteins, and Gc was also produced as two truncated forms, which consisted of its amino-terminal third and carboxyl-terminal two-thirds. The sera from convalescent animals reacted only against the full-length Gc and its subdomains and not against the SBV glycoprotein Gn. Interestingly, the amino-terminal domain of SBV-Gc was targeted not only by polyclonal sera but also by the majority of murine mAbs with a neutralizing activity. Furthermore, the newly defined amino-terminal domain of about 230 aa of the SBV Gc protein could be affinity-purified and further characterized. This major neutralizing domain might be relevant for the development of prophylactic, diagnostic and therapeutic approaches for SBV and other orthobunyaviruses.

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2016-03-01
2020-01-23
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