NEURAMINIDASE OF INFLUENZA A VIRUS: STUDIES ON IMMUNOGENICITY AND INTERACTION WITH OTHER VIRAL PROTEINS AND LIPID.
Item
-
Title
-
NEURAMINIDASE OF INFLUENZA A VIRUS: STUDIES ON IMMUNOGENICITY AND INTERACTION WITH OTHER VIRAL PROTEINS AND LIPID.
-
Identifier
-
AAI8203272
-
identifier
-
8203272
-
Creator
-
DAVIS, JUDITH FITZPATRICK.
-
Contributor
-
Dr. Doris J. Bucher
-
Date
-
1981
-
Language
-
English
-
Publisher
-
City University of New York.
-
Subject
-
Biology, Microbiology
-
Abstract
-
Development of an affinity isolation procedure for the neuraminidase (NA) of influenza A virus (Bucher, 1977), allowed purification of neuraminidase under conditions which preserved the native conformation of the protein, as assayed by enzyme activity. The advantage of enzyme activity as a sensitive index of protein conformation allowed NA to be used as a model for determining conformational requirements for immunogenicity of membrane glycoproteins.;Highly immunogenic preparations of purified neuraminidase were prepared by aggregation of the protein into protein micelles or by association with liposomes: non-aggregated neuraminidase was shown to be only poorly immunogenic. Specific activity of purified neuraminidase varied with conformation but did not correlate with immunogenicity.;M protein was incorporated into a discrete population of heavy density (d 1.22gm/ml) liposomes in a manner that suggested cooperative interaction of M protein during liposomal formation, i.e. preferential association of protein as opposed to random association of protein with lipid which would produce a heterogeneous population of lighter liposomes. This suggested that the formation of M protein domains on the inner surface of influenza virus infected cells might function to provide recognition sites for the viral glycoproteins.;Neuraminidase was only poorly incorporated into liposomes carrying a negative charge, resulting in the formation of light density liposomes and aggregates that did not appear to contain any lipid. In the presence of M protein the incorporation of neuraminidase into liposomes was enhanced; heavy density liposomes which contained both NA and M protein were formed. The high specific activity of neuraminidase-M protein liposomes suggests that neuraminidase-M protein interaction affected neuraminidase conformation.;Hemagglutinin and the HA(,2) polypeptide of hemagglutinin were both shown to be incorporated into lipid in a manner that was suggestive of cooperative interaction. In the presence of M protein a discrete population of heavy density liposomes were formed with both proteins, indicating that both HA and HA(,2) could associate with M to form HA-M protein liposomes and HA(,2)-M protein liposomes.;Liposomal systems containing one or more influenza virus proteins appear to offer a valuable tool for investigation of the mechanisms by which virus assembly proceeds, and may well prove valuable tools in the design and development of specific antiviral agents.
-
Type
-
dissertation
-
Source
-
PQT Legacy CUNY.xlsx
-
degree
-
Ph.D.
-
Program
-
Biomedical Sciences
