Antibody Response to Varicella-Zoster Virus Surface Glycoproteins in Chickenpox and Shingles

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Abstract
Varicella-zoster virus (VZV)-infected cell surface proteins were investigated using extrinsic radiolabeling of the cell surface, immunoprecipitation of detergent-solubilized extract of the same cell surface and fractionation of the immunoprecipitates using SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis). Glycosylated proteins were identified by their affinity for Ricinus communis lectin. Six glycoproteins with apparent MW of 170K (170,000), 105K, 93K, 81K, 53K anfd 45K were identified. The 170K glycoprotein was shown to be disulfide-linked since under reducing conditions for SDS-PAGE it was cleaved to a protein of 63K MW. The IgG responses to these glycoproteins during various clinical circumstances are described. In acute sera from all chickenpox patients and in the majority of acute shingles sera, antibodies reactive with glycoproteins could not be detected. In chickenpox convalescence, antibodies reactive with glycoproteins of MW 170K, 105K, 53K and 45K were identified, while during zoster convalescence antibodies to all 6 were prominent. Antibodies to the disulfide-linked glycoprotein persisted for many years following both the primary disease and its reactivation. Disseminated zoster was associated with significantly low levels of antibodies to these surface glycoproteins.