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PMID: 6091739 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Effect of lipid composition upon fusion of liposomes with Sendai virus membranes.

Biochemistry ·Vol. 23 ·No. 18 ·1984-08-28 ·Pages 4161-6

Haywood AM, Boyer BP

Abstract

How the lipid composition of liposomes determines their ability to fuse with Sendai virus membranes was tested. Liposomes were made of compositions designed to test postulated mechanisms of membrane fusion that require specific lipids. Fusion does not require the presence of lipids that can form micelles such as gangliosides or lipids that can undergo lamellar to hexagonal phase transitions such as phosphatidylethanolamine (PE), nor is a phosphatidylinositol (PI) to phosphatidic acid (PA) conversion required, since fusion occurs with liposomes containing phosphatidylcholine (PC) and any one of many different negatively charged lipids such as gangliosides, phosphatidylserine (PS), phosphatidylglycerol, dicetyl phosphate, PI, or PA. A negatively charged lipid is required since fusion does not occur with neutral liposomes containing PC and a neutral lipid such as globoside, sphingomyelin, or PE. Fusion of Sendai virus membranes with liposomes that contain PC and PS does not require Ca2+, so an anhydrous complex with Ca2+ or a Ca2+-induced lateral phase separation is not required although the possibility remains that viral binding causes a lateral phase separation. Sendai virus membranes can fuse with liposomes containing only PS, so a packing defect between domains of two different lipids is not required. The concentration of PS required for fusion to occur is approximately 10-fold higher than that required for ganglioside GD1a, which has been shown to act as a Sendai virus receptor. When cholesterol is added as a third lipid to liposomes containing PC and GD1a, the amount of fusion decreases if the GD1a concentration is low.(ABSTRACT TRUNCATED AT 250 WORDS)

MeSH Terms
Adsorption Animals Chick Embryo Liposomes Microscopy, Electron Molecular Conformation Parainfluenza Virus 1, Human/metabolism,ultrastructure Protein Binding Structure-Activity Relationship Viral Proteins/metabolism
Chemicals
Liposomes Viral Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Haywood A M
Boyer B P
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1984-08-28
Pages
4161-6
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Grants
NIAID NIH HHS · AI-15540 · United States
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