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 Citation Map 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 Schmidt, M. F. G. Articles by Lambrecht, B. Search for Related Content PubMed PubMed Citation Articles by Schmidt, M. F. G. Articles by Lambrecht, B. Agricola Articles by Schmidt, M. F. G. Articles by Lambrecht, B.

On the Structure of the Acyl Linkage and the Function of Fatty Acyl Chains in the Influenza Virus Haemagglutinin and the Glycoproteins of Semliki Forest Virus

Institut für Virologie, Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, D-6300 Giessen, F.R.G.

The acylation of the haemagglutinin (HA) of different influenza viruses and of the envelope glycoproteins of Semliki Forest virus (SFV) were analysed. The fatty acid linkage in these acylproteins was found to be resistant to a variety of organic solvents and combinations of these, even after pretreatment with various detergents. Fatty acids are released from influenza virus HA at a pH value between 11.8 and 12.1 at room temperature. Although this mild alkaline cleavage occurs rapidly, the release of fatty acids by treatment with hydroxylamine is time-, temperature- and concentration-dependent. By comparison with model esters the linkage in HA is suggested to be of the oxygenester type rather than a thioester linkage. To assay for possible functions of protein-bound fatty acids the biological activities of influenza virus (A/FPV/Rostock/34) and its solubilized spike glycoproteins were measured after deacylation. While viral haemagglutination activity was not hampered at all, its ability to haemolyse erythrocytes and infectivity were drastically reduced. Likewise, viral spike glycoproteins solubilized with detergents failed to induce haemolysis at low pH when fatty acids had been cleaved off. These results indicate the possible involvement of protein-bound fatty acids in fusion inducation through the acylated fusogenic spike glycoproteins.

Keywords: SFV, influenza virus, acylation, glycoproteins, fusion

Received 9 May 1985; accepted 3 September 1985.

This article has been cited by other articles:

				M. A. Kostiuk, M. M. Corvi, B. O. Keller, G. Plummer, J. A. Prescher, M. J. Hangauer, C. R. Bertozzi, G. Rajaiah, J. R. Falck, and L. G. Berthiaume Identification of palmitoylated mitochondrial proteins using a bio-orthogonal azido-palmitate analogue FASEB J, March 1, 2008; 22(3): 721 - 732. [Abstract] [Full Text] [PDF]

				H. J. Kueng, V. M. Leb, D. Haiderer, G. Raposo, C. Thery, S. V. Derdak, K. G. Schmetterer, A. Neunkirchner, C. Sillaber, B. Seed, et al. General Strategy for Decoration of Enveloped Viruses with Functionally Active Lipid-Modified Cytokines J. Virol., August 15, 2007; 81(16): 8666 - 8676. [Abstract] [Full Text] [PDF]

				R. Mora, E. Rodriguez-Boulan, P. Palese, and A. Garcia-Sastre Apical Budding of a Recombinant Influenza A Virus Expressing a Hemagglutinin Protein with a Basolateral Localization Signal J. Virol., March 7, 2002; 76(7): 3544 - 3553. [Abstract] [Full Text] [PDF]

				W. F. Pickl, F. X. Pimentel-Muinos, and B. Seed Lipid Rafts and Pseudotyping J. Virol., August 1, 2001; 75(15): 7175 - 7183. [Abstract] [Full Text]

				F.-Y. Zeng and P. H. Weigel Hydroxylamine Treatment Differentially Inactivates Purified Rat Hepatic Asialoglycoprotein Receptors and Distinguishes Two Receptor Populations J. Biol. Chem., September 8, 1995; 270(36): 21388 - 21395. [Abstract] [Full Text] [PDF]