Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium; the role of the host cell in selection of hemagglutinin receptor specificity
Identifieur interne : 001E75 ( Main/Exploration ); précédent : 001E74; suivant : 001E76Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium; the role of the host cell in selection of hemagglutinin receptor specificity
Auteurs : J. Nelson S. S. Couceiro [Brésil] ; James C. Paulson [États-Unis] ; Linda G. Baum [États-Unis]Source :
- Virus Research [ 0168-1702 ] ; 1993.
English descriptors
- Teeft :
- Apical, Apical surface, Avian, Avian strains, Biol, Cell surface, Chem, Derivatized, Derivatized erythrocytes, Different receptor specificities, Droplet, Epithelial, Epithelial surface, Epithelium, Erythrocyte, Glycoprotein, Goblet, Goblet cells, Hemagglutination, Hemagglutinin, Hemagglutinin receptor specificity, Horse serum, Host cells, Host range, Human influenza, Human mucin, Human trachea, Human tracheal epithelium, Influenza, Influenza virus, Influenza virus strains, Intracellular mucin droplets, Lectin, Linkage, Mucin, Mucin droplets, Paulson, Receptor, Receptor specificity, Room temperature, Sialic, Sialic acid, Sialyloligosaccharides, Tissue sections, Trachea, Trachea sections, Tracheal, Tracheal epithelium, Virus, Virus strain, Virus strains.
Abstract
Abstract: The complement of sialyloligosaccharides present on the surface of human tracheal epithelium has been implicated as an important factor in the selection of hemagglutinin receptor specificity of human influenza A virus. Human strains of influenza A virus preferentially recognize host cell receptors bearing SAα2,6Gal sequences, a sequence which is found on the surface of ciliated tracheal epithelium. A fluorescently-labelled H3 human virus strain bound avidly to the apical surface of human tracheal epithelium, while a fluorescently-labelled receptor variant strain, which preferentially binds SAα2,3Gal sequences, showed little binding to the epithelial surface and localized primarily to intracellular mucin droplets. Extracts of human bronchial mucin, which is known to contain sialic acid primarily in the SAα2,3Gal linkage, was a potent inhibitor of the binding of the receptor variant strain to trachea sections, while the binding of the parent strain was unaffected by the presence of mucin. Human bronchial mucin also inhibited the binding of the receptor variant strains, but not the parent virus strains, to human erythrocytes derivatized to contain SAα2,6Gal sequences. These results suggest that a combination of selection pressures present in the respiratory tract environment have resulted in the evolution of a hemagglutinin receptor specificity in human influenza A virus strains which optimizes recognition of, binding to and infection of host cells.
Url:
DOI: 10.1016/0168-1702(93)90056-S
Affiliations:
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Human strains of influenza A virus preferentially recognize host cell receptors bearing SAα2,6Gal sequences, a sequence which is found on the surface of ciliated tracheal epithelium. A fluorescently-labelled H3 human virus strain bound avidly to the apical surface of human tracheal epithelium, while a fluorescently-labelled receptor variant strain, which preferentially binds SAα2,3Gal sequences, showed little binding to the epithelial surface and localized primarily to intracellular mucin droplets. Extracts of human bronchial mucin, which is known to contain sialic acid primarily in the SAα2,3Gal linkage, was a potent inhibitor of the binding of the receptor variant strain to trachea sections, while the binding of the parent strain was unaffected by the presence of mucin. Human bronchial mucin also inhibited the binding of the receptor variant strains, but not the parent virus strains, to human erythrocytes derivatized to contain SAα2,6Gal sequences. These results suggest that a combination of selection pressures present in the respiratory tract environment have resulted in the evolution of a hemagglutinin receptor specificity in human influenza A virus strains which optimizes recognition of, binding to and infection of host cells.</div></front></TEI><affiliations><list><country><li>Brésil</li><li>États-Unis</li></country><region><li>Californie</li><li>État de Rio de Janeiro</li></region><settlement><li>Rio de Janeiro</li></settlement></list><tree><country name="Brésil"><region name="État de Rio de Janeiro"><name sortKey="Couceiro, J Nelson S S" sort="Couceiro, J Nelson S S" uniqKey="Couceiro J" first="J. Nelson S. S." last="Couceiro">J. Nelson S. S. Couceiro</name></region></country><country name="États-Unis"><region name="Californie"><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name></region><name sortKey="Baum, Linda G" sort="Baum, Linda G" uniqKey="Baum L" first="Linda G." last="Baum">Linda G. Baum</name><name sortKey="Baum, Linda G" sort="Baum, Linda G" uniqKey="Baum L" first="Linda G." last="Baum">Linda G. Baum</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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