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PMID: 6823748 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Chemical and immunological analysis of the rabies soluble glycoprotein.

Virology ·Vol. 124 ·No. 2 ·1983-01-30 ·Pages 330-7

Dietzschold B, Wiktor TJ, Wunner WH, Varrichio A

Abstract

Soluble glycoprotein (Gs), purified from virion-depleted, rabies-infected tissue culture fluid, was chemically and immunologically analyzed. A comparison of this antigen with the virion-associated glycoprotein showed that Gs lacks 58 amino acid residues from the carboxy terminus of the virion-associated glycoprotein. Analysis with monoclonal antibodies revealed that all the epitopes of the viral glycoprotein are also present in the soluble glycoprotein. However, when tested for its ability to protect mice against a lethal challenge infection with rabies virus, Gs in contrast to viral glycoprotein, showed no protective activity. These results suggest that the carboxy terminus of the rabies virus glycoprotein is necessary for its full protective activity even though this portion of the glycoprotein molecule does not contain any antigenic determinants.

MeSH Terms
Animals Glycoproteins/analysis,immunology,isolation & purification Immunization Mice Molecular Weight Rabies/prevention & control Rabies virus/analysis Solubility Structure-Activity Relationship Viral Proteins/analysis,immunology,isolation & purification
Chemicals
Glycoproteins Viral Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Dietzschold B
Wiktor T J
Wunner W H
Varrichio A
Article Info
Journal
Virology
Abbr.
Virology
ISSN
0042-6822
Published
1983-01-30
Pages
330-7
Language
English
Region
United States
NLM ID
0110674
Subset
IM
Grants
NIAID NIH HHS · AI-09706 · United States
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