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 Rau, S. Articles by Friedrich, R. W. Search for Related Content PubMed PubMed Citation Articles by Rau, S. Articles by Friedrich, R. W. Agricola Articles by Rau, S. Articles by Friedrich, R. W.

The role of gp55 N-glycosylation in pathogenesis of Friend spleen focus-forming virus

¹ Institute of Medical Virology, Justus Liebig University, Frankfurter Strasse 107, W-6300 Giessen
and² Institute of Biochemistry, Justus Liebig University, Friedrichstrasse 24, W-6300 Giessen, Germany

The product of the envelope gene (gp55) of Friend spleen focus-forming virus is responsible for the acute form of erythroleukaemia caused by this virus. In order to investigate the role that the four known N-linked carbohydrate side-chains of gp55 play in pathogenesis, we have inactivated the four N-glycosylation signals by mutating the asparagine residues of these four sites into serine. When glycosylation sites 1 and/or 2 were altered, the viruses remained fully pathogenic. However, mutation at either of glycosylation sites 3 or 4 rendered the virus apathogenic, independent of mutations at other sites. Furthermore, when site 3 was changed, a new product appeared which seemed to have acquired a carbohydrate chain at a position normally not glycosylated, presumably at position Asn₃₇₈.

Received 30 September 1992; accepted 20 November 1992.

This article has been cited by other articles:

				L. Kasturi, J. R. Eshleman, W. H. Wunner, and S. H. Shakin-Eshleman The Hydroxy Amino Acid in an Asn-X-Ser/Thr Sequon Can Influence N-Linked Core Glycosylation Efficiency and the Level of Expression of a Cell Surface Glycoprotein J. Biol. Chem., June 16, 1995; 270(24): 14756 - 14761. [Abstract] [Full Text] [PDF]