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Neutralization epitope of varicella zoster virus on native viral glycoprotein gp118 (VZV glycoprotein gplll)
Journal article   Peer reviewed

Neutralization epitope of varicella zoster virus on native viral glycoprotein gp118 (VZV glycoprotein gplll)

Eduardo A Montalvo and Charles Grose
Virology (New York, N.Y.), Vol.149(2), pp.230-241
1986
DOI: 10.1016/0042-6822(86)90124-8
PMID: 2418586

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Abstract

Varicella-zoster virus (VZV) specifies the formation of several glycoproteins, including a 118,000-Da mature structural product (gp118). The biologic and biochemical properties of gp118 were studied after production of murine monoclonal antibodies to both a low-passage laboratory strain (VZV-32) and an attenuated vaccine strain (VZV-Oka). Structural analyses performed with the three glycosidases endo-(β- N-acetylglucosaminidase H (endoglycosidase H), endo-β- N-acetylglucosaminidase F (endoglycosidase F), and endo-α- N-acetylgalactosaminidase demonstrated that gp118 was predominantly an N-linked complex type glycoprotein built upon a polypeptide backbone of approximately 79,000 Da. Sialic acid residues were present on the mature glycoprotein, but these terminal sugars were absent from the partially glycosylated intermediate forms recovered from monensin-treated infected cultures. Unlike another VZV-specified glycoprotein gp98, no new oligosaccharide moieties were observed on gp118 after addition of tunicamycin to VZV-infected cultures. By plaque reduction assays with a panel of monoclonal antibodies, we defined an epitope on this glycoprotein which elicited a complement-independent neutralizing antibody response of high magnitude. The epitope was highly conserved, since it was present on a laboratory VZV strain, wild type isolates, as well as the attenuated vaccine strain (VZV-Oka). Competitive blocking experiments with the same anti-gp118 monoclonal antibodies indicated that four neutralizing antibodies were directed against similar or identical epitopes whereas one nonneutralizing antibody reacted with a different antigenic site. Thus, this study demonstrates the presence of an immunodominant neutralization epitope on native viral glycoprotein gp118. Under a new consensus nomenclature, this glycoprotein will be designated VZV gpIII.

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