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Title: Carbohydrates of influenza virus. I. Glycopeptides derived from viral glycoproteins after labeling with radioactive sugars. [/sup 14/C, /sup 3/H]

Abstract

The carbohydrate moiety of the influenza glycoproteins NA, HA/sub 1/, and HA/sub 2/ were analyzed by labeling with radioactive sugars. Analysis of glycopeptides obtained after digestion with Pronase indicated that there are at least two different types of carbohydrate side chains. The side chain of type I is composed of glucosamine, mannose, galactose, and fucose. It is found on NA, HA/sub 1/, and HA/sub 2/. The side chain of type II contains a high amount of mannose and is found only on NA and HA/sub 2/. The molecular weights of the corresponding glycopeptides obtained from virus grown in chicken ambryo cells are 2,600 for type I and 2,000 for type II. The glycoproteins of virus grown in MDBK cells have a higher molecular weight than those of virus grown in chicken embryo cells, and there is a corresponding difference in the molecular weights of the glycopeptides. Under conditions of partial inhibition of glycosylation, virus particles were isolated that contained hemagglutinin with reduced carbohydrate content. Glycopeptide analysis indicated that this reduction is due to the lack of whole carbohydrate side chains and not to the incorporation of incomplete ones. This observation suggests that glycosylation of the viral glycoproteins involves en blocmore » transfer of the core sugars to the polypeptide chains.« less

Authors:
; ; ;
Publication Date:
Research Org.:
Univ., Giessen, Germany
OSTI Identifier:
7312212
Resource Type:
Journal Article
Journal Name:
J. Virol.; (United States)
Additional Journal Information:
Journal Volume: 23:2
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; CARBOHYDRATES; BIOCHEMICAL REACTION KINETICS; RADIONUCLIDE KINETICS; GLUCOPROTEINS; INFLUENZA VIRUSES; SACCHARIDES; CARBON 14; LABELLING; MOLECULAR WEIGHT; TRITIUM; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; CARBON ISOTOPES; EVEN-EVEN NUCLEI; HYDROGEN ISOTOPES; ISOTOPES; KINETICS; LIGHT NUCLEI; MICROORGANISMS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; PARASITES; PROTEINS; RADIOISOTOPES; REACTION KINETICS; VIRUSES; YEARS LIVING RADIOISOTOPES; 550200* - Biochemistry; 560174 - Radiation Effects- Nuclide Kinetics & Toxicology- Microorganisms- (-1987)

Citation Formats

Schwarz, R T, Schmidt, M F.G., Anwer, U, and Klenk, H D. Carbohydrates of influenza virus. I. Glycopeptides derived from viral glycoproteins after labeling with radioactive sugars. [/sup 14/C, /sup 3/H]. United States: N. p., 1977. Web.
Schwarz, R T, Schmidt, M F.G., Anwer, U, & Klenk, H D. Carbohydrates of influenza virus. I. Glycopeptides derived from viral glycoproteins after labeling with radioactive sugars. [/sup 14/C, /sup 3/H]. United States.
Schwarz, R T, Schmidt, M F.G., Anwer, U, and Klenk, H D. Mon . "Carbohydrates of influenza virus. I. Glycopeptides derived from viral glycoproteins after labeling with radioactive sugars. [/sup 14/C, /sup 3/H]". United States.
@article{osti_7312212,
title = {Carbohydrates of influenza virus. I. Glycopeptides derived from viral glycoproteins after labeling with radioactive sugars. [/sup 14/C, /sup 3/H]},
author = {Schwarz, R T and Schmidt, M F.G. and Anwer, U and Klenk, H D},
abstractNote = {The carbohydrate moiety of the influenza glycoproteins NA, HA/sub 1/, and HA/sub 2/ were analyzed by labeling with radioactive sugars. Analysis of glycopeptides obtained after digestion with Pronase indicated that there are at least two different types of carbohydrate side chains. The side chain of type I is composed of glucosamine, mannose, galactose, and fucose. It is found on NA, HA/sub 1/, and HA/sub 2/. The side chain of type II contains a high amount of mannose and is found only on NA and HA/sub 2/. The molecular weights of the corresponding glycopeptides obtained from virus grown in chicken ambryo cells are 2,600 for type I and 2,000 for type II. The glycoproteins of virus grown in MDBK cells have a higher molecular weight than those of virus grown in chicken embryo cells, and there is a corresponding difference in the molecular weights of the glycopeptides. Under conditions of partial inhibition of glycosylation, virus particles were isolated that contained hemagglutinin with reduced carbohydrate content. Glycopeptide analysis indicated that this reduction is due to the lack of whole carbohydrate side chains and not to the incorporation of incomplete ones. This observation suggests that glycosylation of the viral glycoproteins involves en bloc transfer of the core sugars to the polypeptide chains.},
doi = {},
url = {https://www.osti.gov/biblio/7312212}, journal = {J. Virol.; (United States)},
number = ,
volume = 23:2,
place = {United States},
year = {1977},
month = {8}
}