This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Williams, M A Articles by Lamb, R A Search for Related Content PubMed PubMed Citation Articles by Williams, M A Articles by Lamb, R A

 Previous Article  |  Next Article 

Mol Cell Biol. 1988 March; 8(3): 1186-1196

Polylactosaminoglycan modification of a small integral membrane glycoprotein, influenza B virus NB.

Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208.

ABSTRACT

The structure of the carbohydrate components of NB, the small integral membrane glycoprotein of influenza B virus, was investigated. The carbohydrate chains of NB are processed from the high-mannose form (NB18) to a heterogeneous form of much higher molecular weight, designated NBp. Selection of this carbohydrate-containing form of NB with Datura stramonium lectin, its susceptibility to digestion by endo-beta-galactosidase, and determination of the size of NBp glycopeptides by gel filtration chromatography suggested that the increase in molecular weight is due to processing to polylactosaminoglycan. Investigation of the polypeptides produced by influenza B/Lee/40 virus infection of several cell types and another strain of influenza B virus suggested that the signal for modification to polylactosaminoglycan is contained in NB. Expression of mutants of NB lacking either one or both of the normal N-terminal sites of asparagine-linked glycosylation indicated that both carbohydrate chains are modified to contain polylactosaminoglycan. NBp and a small amount of unprocessed NB18 are expressed at the infected-cell surface, as determined by digestion of the surfaces of intact cells with various endoglycosidases. Unglycosylated NB, expressed either in influenza B virus-infected cells treated with tunicamycin or in cells expressing the NB mutant lacking both N-linked glycosylation sites, was expressed at the cell surface, indicating that NB does not require carbohydrate addition for transport.

This article has been cited by other articles:

• Robertson, S. J., Ammann, C. G., Messer, R. J., Carmody, A. B., Myers, L., Dittmer, U., Nair, S., Gerlach, N., Evans, L. H., Cafruny, W. A., Hasenkrug, K. J. (2008). Suppression of Acute Anti-Friend Virus CD8+ T-Cell Responses by Coinfection with Lactate Dehydrogenase-Elevating Virus. J. Virol. 82: 408-418 [Abstract] [Full Text]  
• Hatta, M., Kawaoka, Y. (2003). The NB Protein of Influenza B Virus Is Not Necessary for Virus Replication In Vitro. J. Virol. 77: 6050-6054 [Abstract] [Full Text]  
• Pekosz, A., Lamb, R. A. (1998). Influenza C virus CM2 integral membrane glycoprotein is produced from a polypeptide precursor by cleavage of an internal signal sequence. Proc. Natl. Acad. Sci. USA 95: 13233-13238 [Abstract] [Full Text]  
• Parks, G. D., Parks, G. D. (1996). Differential Effects of Changes in the Length of a Signal/Anchor Domain on Membrane Insertion, Subunit Assembly, and Intracellular Transport of a Type II Integral Membrane Protein. J. Biol. Chem. 271: 7187-7195 [Abstract] [Full Text]