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PMID: 6310862 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Evidence for different receptor sites in mouse spleen cells for the Sendai virus hemagglutinin-neuraminidase (HN) and fusion (F) glycoproteins.

Virology ·Vol. 128 ·No. 2 ·1983-07-30 ·Pages 366-76

Peterhans E, Baechi T, Yewdell J

Abstract

Liposomes were reconstituted from phosphatidylcholine and Sendai virus glycoproteins HN or F and their interaction with mouse spleen cells was studied. Both the HN and F liposomes were able to stimulate chemiluminescence (CL), indicating that the glycoproteins were able to interact with the cell membrane independently of each other. The induction of CL in cells which had been pretreated with liposomes by monoclonal antibodies to either HN or F demonstrated that HN and F bind to the cells independently. The presence of F liposomes on the cell surface was also confirmed by immunoelectron microscopy. Cells pretreated with HN and F liposomes revealed a different pattern of CL when challenged with intact virus or the calcium ionophore A23187 indicating that HN and F bind to different receptor sites.

MeSH Terms
Binding Sites Cell Membrane/metabolism HN Protein Liposomes Luminescent Measurements Parainfluenza Virus 1, Human/analysis Receptors, Virus/metabolism Spleen/cytology,metabolism Viral Fusion Proteins Viral Proteins/metabolism
Chemicals
HN Protein HN protein receptor Liposomes Receptors, Virus Viral Fusion Proteins Viral Proteins virus fusion protein receptor, Sendai virus
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Peterhans E
Baechi T
Yewdell J
Article Info
Journal
Virology
Abbr.
Virology
ISSN
0042-6822
Published
1983-07-30
Pages
366-76
Language
English
Region
United States
NLM ID
0110674
Subset
IM
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