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J Gen Virol 66 (1985), 1785-1793; DOI 10.1099/0022-1317-66-8-1785
© 1985 Society for General Microbiology

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

Margot Larkin, John E. Heckels and Marie M. Ogilvie

Department of Microbiology, University of Southampton Medical School, Southampton General Hospital, Southampton SO9 4XY, U.K.

Varicella-zoster virus (VZV)-infected cell surface proteins were investigated using extrinsic radiolabelling of the cell surface, immunoprecipitation of detergent-solubilized extract of the same cell surface and fractionation of the immunoprecipitates using SDS-PAGE. Glycosylated proteins were identified by their affinity for Ricinus communis lectin. Six glycoproteins with apparent mol. wt. of 170K, 105K, 93K, 81K, 53K and 45K were identified. The 170K glycoprotein was shown to be disulphidelinked since under reducing conditions for SDS-PAGE it was cleaved to a protein of 63K mol. wt. 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 mol. wt. 170K, 105K, 53K and 45K were identified, whilst during zoster convalescence antibodies to all six were prominent. Antibodies to the disulphide-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.

Keywords: VZV, surface glycoproteins, radioimmunoprecipitation, immunoglobulin response

Received 14 January 1985; accepted 8 May 1985.





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Copyright © 1985 by the Society for General Microbiology.