A herpes simplex virus type 2 (HSV-2) type-specific monoclonal antibody (MAb), CH-A9, precipitated a glycoprotein with an of approximately 30000 (g30K) from extracts of HSV-2-infected BHK cells labelled with [H]leucine, [C]fructose or [H]glucosamine. The of this glycoprotein is lower than those of other HSV glycoproteins. Immunoassays of BHK cells infected with HSV-1-HSV-2 intertypic recombinants localized the gene encoding the target antigen of MAb CH-A9 to the unique long (U) region at map units 0.490 to 0.564. Tunicamycin effectively inhibits -linked glycosylation of g30K, which suggests that g30K may be modified by addition of -linked oligosaccharides and that the amino acid sequence may contain Asn-X-Ser or Asn-X-Thr. The g30K was also purified on an immunoadsorbent column consisting of MAb CH-A9 linked to Sepharose 4B and was shown to be an HSV-2 type-specific antigen by indirect ELISA. The glycoprotein could induce HSV-2 type-specific neutralizing antibody in BALB/c mice. This evidence suggests that g30K may be a novel glycoprotein of HSV-2.


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