Summary auto-generated
This study characterized the antigenic properties of human herpesvirus 7 (HHV-7) using antibodies from patients with exanthem subitum, immunized mice, and monoclonal antibodies (MAbs). Radiolabeled HHV-7-infected cell lysates were analyzed by immunoprecipitation and SDS-PAGE. Human convalescent sera recognized 9-16 HHV-7-specific polypeptides (26-210 kDa), with a prominent 52 kDa protein. Mouse immune sera detected over 18 polypeptides with similar molecular mass ranges. Forty-two MAb-producing hybridoma clones were established, and seven were characterized in detail. Two MAbs (5E12 and 5F12) showed neutralizing activity and recognized distinct glycoproteins of 78 and 85 kDa, respectively, indicating at least two neutralization-inducing epitopes. MAb 16B4 recognized the major 52 kDa immunogenic protein. Some MAbs exhibited cross-reactivity with HHV-6, with five of 42 MAbs reacting to both viruses in immunofluorescence assays. MAb 7C10 cross-reacted with an HHV-6 protein of 45 kDa while recognizing the HHV-7 40 kDa protein. These findings demonstrate that HHV-7 is immunologically distinct from HHV-6 despite limited cross-reactivity at certain epitopes.
Key findings
- At least 16 HHV-7-specific polypeptides (26-210 kDa) were identified by human convalescent sera, with a 52 kDa protein being the most prominent and immunogenic
- Two MAbs (5E12 and 5F12) possessed neutralizing activity against HHV-7 and recognized distinct glycoproteins of 78 kDa and 85 kDa, suggesting multiple neutralization-inducing epitopes
- Limited antigenic cross-reactivity exists between HHV-7 and HHV-6, with five of 42 MAbs reacting to both viruses despite HHV-7 being immunologically distinct from HHV-6
- MAb 16B4 specifically recognized the major 52 kDa immunogenic protein without cross-reacting with HHV-6
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Abstract
Using polyclonal and monoclonal (MAbs) antibodies to human herpesvirus 7 (HHV-7), we have studied HHV-7-specific polypeptides. Human sera were obtained during the convalescent phase from patients with exanthem subitum due to HHV-7, and at least 16 HHV-7-specific polypeptides with apparent molecular masses of 26-210 kDa were immuno-precipitated. Sera prepared in mice also precipitated at least 17 HHV-7-specific polypeptides with molecular masses of 26-210 kDa. Among them, the most commonly observed antigenic protein had an apparent molecular mass of 52 kDa. Forty-two clones secreting MAbs against HHV-7-specific proteins, as determined by immunofluorescence assays, were established from BALB/c mice immunized with HHV-7-infected cell extracts. Seven MAbs which immunoprecipitated HHV-7-specific polypeptides were further characterized. Two of these, MAbs 5E12 and 5F12, reacted predominantly with glyco-proteins of 78 kDa and 85 kDa, respectively, and possessed neutralizing activity. This suggests that there are at least two neutralization-inducing proteins in HHV-7. MAb 16B4 reacted with the major immunogenic protein of 52 kDa. Five of the 42 MAbs also reacted in immunofluorescence assays with HHV-6 antigens to the same degree as to HHV-7. Two other MAbs, 7C10 and 10F1, recognized an HHV-7 protein of 40 kDa, and only 7C10 cross-reacted with an HHV-6 protein of 45 kDa.