H2N2V1, Main, Exploration, bibRecord, 002426

Sialic acid is incorporated into influenza hemagglutinin glycoproteins in the absence of viral neuraminidase

Identifieur interne : 002426 ( Main/Exploration ); précédent : 002425; suivant : 002427

Sialic acid is incorporated into influenza hemagglutinin glycoproteins in the absence of viral neuraminidase

Auteurs : Sukla Basak [États-Unis] ; Milan Tomana [États-Unis] ; Richard W. Compans [États-Unis]

Source :

Virus Research [ 0168-1702 ] ; 1985.

RBID : ISTEX:7626E7887493E467B3615EF3EED69A7FDAD30601

Descripteurs français

Pascal (Inist)
- Clonage moléculaire, Enzyme, Glycoprotéine, Hémagglutination, Influenzavirus A, Neuraminidase, Sialique acide, Virus SV40.
Wicri :
- topic : Enzyme.

English descriptors

KwdEn :
- Enzyme, Glycoproteins, Hemagglutination, Influenzavirus A, Molecular cloning, Neuraminidase, SV40 virus, Sialic acid.
Teeft :
- Carbohydrate, Cdna copies, Compans, Glycopeptides, Glycoprotein, Hazoa, Hemagglutinin, Influenza, Influenza virions, Influenza virus, Neuraminidase, Neuraminidase treatment, Oligosaccharide, Palese, Sialic, Sialic acid, Vesicular stomatitis virus, Viral, Virion, Virology.

Abstract

Abstract: We have analyzed the pronase-derived glycopeptides of the hemagglutinin glycoproteins expressed from SV40 vectors carrying cloned cDNA copies of the HA gene and of HA isolated from influenza virions (A/Jap/305/57). The glycopeptides derived from the HA glycoprotein obtained from cloned genes were heterogeneous, ranging in size from 3800 to 2800 dallons. Upon treatment with neuraminidase, sialic acid was released from the glycopeptides and their size was reduced to 2900–2400 daltons. However, under the same conditions, no sialic acid was detected in the virion HA. The presence of sialic acid was confirmed by monosaccharide analysis of the HA glycoprotein derived from products of cloned genes. These results support the idea that during replication of influenza virus, the viral neuraminidase cleaves sialic acid from the HA glycoprotein in infected cells.

Url:

https://api.istex.fr/ark:/67375/6H6-8JPZVZ69-N/fulltext.pdf

DOI: 10.1016/0168-1702(85)90060-7

Affiliations:

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<front><div type="abstract" xml:lang="en">Abstract: We have analyzed the pronase-derived glycopeptides of the hemagglutinin glycoproteins expressed from SV40 vectors carrying cloned cDNA copies of the HA gene and of HA isolated from influenza virions (A/Jap/305/57). The glycopeptides derived from the HA glycoprotein obtained from cloned genes were heterogeneous, ranging in size from 3800 to 2800 dallons. Upon treatment with neuraminidase, sialic acid was released from the glycopeptides and their size was reduced to 2900–2400 daltons. However, under the same conditions, no sialic acid was detected in the virion HA. The presence of sialic acid was confirmed by monosaccharide analysis of the HA glycoprotein derived from products of cloned genes. These results support the idea that during replication of influenza virus, the viral neuraminidase cleaves sialic acid from the HA glycoprotein in infected cells.</div>
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Sialic acid is incorporated into influenza hemagglutinin glycoproteins in the absence of viral neuraminidase

Sialic acid is incorporated into influenza hemagglutinin glycoproteins in the absence of viral neuraminidase

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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