Dynamic properties of Newcastle Disease Virus envelope and their relations with viral hemagglutinin-neuraminidase membrane glycoprotein
- PMID: 9247163
- DOI: 10.1016/s0005-2736(97)00040-0
Dynamic properties of Newcastle Disease Virus envelope and their relations with viral hemagglutinin-neuraminidase membrane glycoprotein
Abstract
The lipid composition of Newcastle Disease Virus (NDV) Clone-30 strain shows a low lipid/protein ratio, a high cholesterol/phospholipid molar ratio, and major phospholipids being qualitatively different to other NDV strains. The major fatty acyl constituents are palmitic, stearic, oleic, and linoleic acids; cerebrosides, sulfatides and two kinds of gangliosides are also found in the NDV membrane. It is reported for the first time in NDV that phospholipid classes are asymmetrically distributed over the two leaflets of the membrane: 60 +/- 4.5% of the phosphatidylcholine and 70 +/- 5.0% of the sphingomyelin are in the outer monolayer. Intact viral membranes and reconstituted NDV envelopes showed similar dynamic properties. Hemagglutinin-neuraminidase (HN) and fusion (F) proteins of NDV membrane affect the lipid thermotropic behaviour in reconstituted proteoliposomes made up of a single class of phospholipids. It is shown that the lipid composition is more important than the bulk membrane fluidity/order for both sialidase (neuraminidase) and hemagglutinating HN activities. Sialidase and hemagglutinating activities requires the presence of definite phospholipids (phosphatidylethanolamine) in its environment.
Similar articles
-
Topological location and biological significance of phospholipids in the membrane of Newcastle disease virus. Hydrolysis of phospholipids in intact virion with pure phospholipases A2, C, and D.J Biochem. 1982 Aug;92(2):575-83. doi: 10.1093/oxfordjournals.jbchem.a133966. J Biochem. 1982. PMID: 7130158
-
Conformational changes of Newcastle disease virus envelope glycoproteins triggered by gangliosides.Eur J Biochem. 2004 Feb;271(3):581-8. doi: 10.1111/j.1432-1033.2003.03960.x. Eur J Biochem. 2004. PMID: 14728685
-
Fusogenic activity of reconstituted newcastle disease virus envelopes: a role for the hemagglutinin-neuraminidase protein in the fusion process.Int J Biochem Cell Biol. 2002 Apr;34(4):403-13. doi: 10.1016/s1357-2725(01)00127-3. Int J Biochem Cell Biol. 2002. PMID: 11854039
-
Nucleotide and predicted amino acid sequence analysis of the fusion protein and hemagglutinin-neuraminidase protein genes among Newcastle disease virus isolates. Phylogenetic relationships among the Paramyxovirinae based on attachment glycoprotein sequences.Funct Integr Genomics. 2004 Oct;4(4):246-57. doi: 10.1007/s10142-004-0113-2. Epub 2004 Apr 24. Funct Integr Genomics. 2004. PMID: 15108051
-
Newcastle Disease Virus Establishes Persistent Infection in Tumor Cells In Vitro: Contribution of the Cleavage Site of Fusion Protein and Second Sialic Acid Binding Site of Hemagglutinin-Neuraminidase.J Virol. 2017 Jul 27;91(16):e00770-17. doi: 10.1128/JVI.00770-17. Print 2017 Aug 15. J Virol. 2017. PMID: 28592535 Free PMC article.
Cited by
-
Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: a minireview.Glycoconj J. 2006 Feb;23(1-2):5-17. doi: 10.1007/s10719-006-5433-0. Glycoconj J. 2006. PMID: 16575518 Review.
-
Cholesterol dependence of Newcastle Disease Virus entry.Biochim Biophys Acta. 2012 Mar;1818(3):753-61. doi: 10.1016/j.bbamem.2011.12.004. Epub 2011 Dec 13. Biochim Biophys Acta. 2012. PMID: 22192779 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources