Summary auto-generated
This study identified a novel linear B-cell epitope at the N-terminal region of rabies virus glycoprotein using phage-display screening and two monoclonal antibodies (mAbs). The epitope, designated WxxxDI, is located between amino acids 14-19 of the mature glycoprotein. Using phage-display library screening, truncated glycoprotein fragments, and synthetic peptides, researchers confirmed the epitope location and showed it is recognized by both original mAbs and sera from some rabies-vaccinated dogs. The epitope sequence is highly conserved among most rabies virus isolates and across lyssavirus phylogroup I (including European bat lyssaviruses), though less conserved in phylogroup II. A 12-amino acid synthetic peptide of this epitope was immunogenic in rabbits and mice when presented in multimeric form, inducing antibody responses in both species. However, antibodies raised against the epitope showed no neutralizing activity against rabies virus, suggesting the epitope may not be surface-exposed under native conditions. The findings indicate potential applications in vaccination screening assays, though a single peptide may be insufficient as a discriminator compared to current methods.
Key findings
- A conserved linear B-cell epitope (WxxxDI) was identified at positions 14-19 of rabies virus glycoprotein N-terminus using phage-display screening of two monoclonal antibodies
- The epitope is highly conserved among most rabies virus isolates worldwide and within lyssavirus phylogroup I but shows greater variation in phylogroup II
- Synthetic peptide mimics of the epitope are recognized by vaccinated dog sera and are immunogenic in rabbits and mice when presented in multimeric form
- Antibodies against the peptide epitope demonstrate no virus-neutralizing activity, suggesting the epitope is likely not surface-exposed under native conditions
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Abstract
A novel, linear B-cell epitope has been identified at the N terminus of the rabies virus (RABV) glycoprotein. Screening of a phage-display library demonstrated that two glycoprotein-specific mAbs recognized a conserved sequence, WxxxDI, which aligned between aa 14 and 19 of the mature glycoprotein. Screening of truncated glycoprotein fragments with both mAbs confirmed the location of the epitope in the N-terminal region. Alignment of amino acid sequences from a range of RABV isolates indicated that the site was conserved in most viruses. Alignment with representatives of other lyssaviruses suggested that it is conserved within phylogroup I, which includes the European bat lyssaviruses, but not phylogroup II. A 12 aa synthetic peptide of this epitope was recognized by both mAbs and sera from a subset of rabies-vaccinated dogs. In a multimeric form, the peptide could induce an epitope-specific response following immunization in rabbits and mice.