Document Detail

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.
MedLine Citation:
PMID:  3934339     Owner:  NLM     Status:  MEDLINE    
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 induction through the acylated fusogenic spike glycoproteins.
M F Schmidt; B Lambrecht
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of general virology     Volume:  66 ( Pt 12)     ISSN:  0022-1317     ISO Abbreviation:  J. Gen. Virol.     Publication Date:  1985 Dec 
Date Detail:
Created Date:  1986-01-21     Completed Date:  1986-01-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0077340     Medline TA:  J Gen Virol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  2635-47     Citation Subset:  IM    
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MeSH Terms
Fatty Acids*
Hemagglutinins, Viral*
Lipoproteins / biosynthesis*,  physiology
Membrane Fusion
Protein Processing, Post-Translational
Semliki forest virus
Structure-Activity Relationship
Viral Envelope Proteins*
Reg. No./Substance:
0/Esters; 0/Fatty Acids; 0/Glycoproteins; 0/Hemagglutinins, Viral; 0/Lipoproteins; 0/Viral Envelope Proteins; 56-45-1/Serine; 72-19-5/Threonine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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