Key result
HPeV1 and HPeV3 conformational epitopes cluster into three sites with consistent distribution but varying residues.
Why the study?
There is a lack of systematic research on the antigenic epitopes of human parechoviruses, which are useful for understanding virus-receptor interactions, developing therapeutics or diagnostics, and monitoring evolution.
Bioinformatics prediction identified key conformational epitopes and specific amino acid residues crucial for monoclonal antibody binding and distinguishing between HPeV1 and HPeV3.
Answers are grounded in this paper and cite their sources.
Epitope predictions may inform HPeV serotype-specific mAb design; leaves open clinical utility pending experimental validation.
Human parechoviruses (HPeVs) are human pathogens that usually cause diseases ranging from rash to neonatal sepsis in young children. HPeV1 and HPeV3 are the most frequently reported genotypes and their three-dimensional structures have been determined. However, there is a lack of systematic research on the antigenic epitopes of HPeVs, which are useful for understanding virus-receptor interactions, developing antiviral agents or molecular diagnostic tools, and monitoring antigenic evolution. Thus, we systematically predicted and compared the conformational epitopes of HPeV1 and HPeV3 using bioinformatics methods in the study. The results showed that both epitopes clustered into three sites (sites 1, 2 and 3). Site 1 was located on the "northern rim" near the fivefold vertex; site 2 was on the "puff"; and site 3 was divided into two parts, of which one was located on the "knob" and the other was close to the threefold vertex. The predicted epitopes highly overlapped with the reported antigenic epitopes, which indicated that the prediction results were accurate. Although the distribution positions of the epitopes of HPeV1 and HPeV3 were highly consistent, the residues varied largely and determined the genotypes. Three amino acid residues, VP3-91N, -92H and VP0-257S, were the key residues for monoclonal antibody (mAb) AM28 binding to HPeV1 and were also of great significance in distinguishing HPeV1 and HPeV3. We also found that two residues, VP1-85N and -87D, might affect the capability of mAb AT12-015 to bind to HPeV3.
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Rong et al. (2021) studied Human parechovirus (HPeV) infection. Bioinformatics-based prediction algorithm was evaluated on Conformational epitopes of HPeV1 and HPeV3. Bioinformatics-based prediction revealed that conformational epitopes of HPeV1 and HPeV3 cluster into three sites with highly consistent distribution patterns but varying residues.
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