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. 1981 Mar;31(3):1044–1053. doi: 10.1128/iai.31.3.1044-1053.1981

Immunogenic glycoproteins of laboratory and vaccine strains of Varicella-Zoster virus.

C Grose, B J Edmond, W E Friedrichs
PMCID: PMC351423  PMID: 6262245

Abstract

High-titered antisera were prepared in guinea pigs and rabbits against two strains of varicella-zoster virus (VZV): VZV-32, a low-passage laboratory strain, and VZV-Oka, a vaccine strain attenuated by passage in both human and guinea pig embryo cells. When the animal VZV-immune sera, as well as a human zoster serum, were used to precipitate radiolabeled glycoproteins from VZV-infected cells and the immune precipitates were analyzed by polyacrylamide gel electrophoresis and fluorography, it was observed that cell cultures infected with either strain had similar electrophoretic profiles containing major glycoproteins of approximate molecular weights 62,000, 98,000, and 118,000. A prominent high-molecular-weight (approximately 150,000) nonglycosylated polypeptide was identified in both strains also. These determinants were demonstrable by both indirect (staphylococcal protein A-antibody adsorbent) and direct immunoprecipitation, as long as VZV-immune sera with an antibody titer greater than or equal to 1:128 were used. Further analysis of individual caviid VZV antisera demonstrated some heterogeneity which appeared to be related to the method of immunization rather than the level of virus-specific antibody. VZV extracts emulsified with complete Freund adjuvant elicited an antibody response to all major immunogenic viral glycoproteins, whereas guinea pigs inoculated with virus alone during the primary immunization initially produced VZV antibody which failed to precipitate the highest-molecular-weight glycoprotein (gp118). Thus, Freund-type adjuvants promoted the maturation of the humoral immune response after VZV immunization in outbred guinea pigs.

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Selected References

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