HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Dietzschold, B. Articles by Koprowski, H. Search for Related Content PubMed PubMed Citation Articles by Dietzschold, B. Articles by Koprowski, H. Agricola Articles by Dietzschold, B. Articles by Koprowski, H.

Isolation and Purification of a Polymeric Form of the Glycoprotein of Rabies Virus

Bernhard Dietzschold^*,

James H. Cox

Lothar G. Schneider

The^* Wistar Institute of Anatomy and Biology, 36th Street at Spruce, Philadelphia, Pennsylvania 19104, U.S.A.
Federal Research Institute for Animal Virus Diseases, Tübingen, Federal Republic of Germany

Of the three major proteins associated with the rabies virus membrane, only the glycoprotein was found to be located on the external surface of the virus membrane. Glycoprotein prepared by treatment of rabies virus with Triton X-100 and purified by isoelectric focusing was found to be homogeneous with respect to size and isoelectric point. This material, which is free of phospholipids, is able to protect in vaccination experiments against a lethal challenge infection with rabies virus. The apparent mol. wt. of this component isolated under non-denaturing conditions is approx. 400000. The same material analysed by SDS polyacrylamide gel electrophoresis (PAGE) was found to consist solely of polypeptide chains of the G protein (mol. wt. 80000). A minor glycoprotein (gp 50), detected by PAGE of the Triton X-100 released material, appeared to be a breakdown product of the G-protein. Therefore the detergent released material represents homopolymers of the G-protein. Whether the antigenic determinants reside on the monomeric subunit or are a property of the polymeric form of the G-protein is discussed.

On leave from the Federal Research Institute for Animal Virus Diseases Tübingen, Federal Republic of Germany.

Received 30 December 1977; accepted 30 January 1978.

This article has been cited by other articles:

				F. Kien, J.-D. Abraham, C. Schuster, and M. P. Kieny Analysis of the subcellular localization of hepatitis C virus E2 glycoprotein in live cells using EGFP fusion proteins J. Gen. Virol., March 1, 2003; 84(3): 561 - 566. [Abstract] [Full Text] [PDF]