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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1988-11-8
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pubmed:abstractText |
Binding experiments with radioactively labelled influenza C virions were carried out to investigate the interaction of the virus with human erythrocytes. The erythrocytes from any of 35 different individuals were found to contain influenza C virus-binding sites though their number was variable among the individuals and was much less than that on mouse, rat and chicken erythrocytes. Attachment of influenza C virus to human erythrocytes was inhibited completely by prior treatment of the virus with anti-HE monoclonal antibody having a strong haemagglutination inhibition activity. Pretreatment of erythrocytes with neuraminidase or the neuraminate-O-acetylesterase of influenza C virus resulted in a marked reduction in the level of virus binding. Thus it appears that human erythrocytes have a low level of O-acetylated sialic acid-containing glycoconjugates that can interact specifically with the HE glycoprotein of influenza C virus. Proteolytic digestion of erythrocytes with ficin, bromelain or V-8 protease inhibited virus binding almost completely, suggesting that the erythrocyte receptor for influenza C virus is a glycoprotein. In contrast to these enzymes, trypsin treatment of erythrocytes reduced virus binding by only about 50%, and alpha-chymotrypsin treatment did not inhibit at all. It was also found that treatment of erythrocytes with monoclonal antibody to the M or N blood group antigen greatly inhibited virus binding to the cells. These results, taken together, suggest that most influenza C virus receptors on human erythrocytes, if not all, reside on glycophorin A which is known to possess the M or N blood group activity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Glycophorin,
http://linkedlifedata.com/resource/pubmed/chemical/MNSs Blood-Group System,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-1317
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
69 ( Pt 10)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2545-53
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3049938-Animals,
pubmed-meshheading:3049938-Antibodies, Monoclonal,
pubmed-meshheading:3049938-Chickens,
pubmed-meshheading:3049938-Erythrocytes,
pubmed-meshheading:3049938-Glycophorin,
pubmed-meshheading:3049938-Hemagglutination Tests,
pubmed-meshheading:3049938-Humans,
pubmed-meshheading:3049938-Influenzavirus C,
pubmed-meshheading:3049938-MNSs Blood-Group System,
pubmed-meshheading:3049938-Neuraminidase,
pubmed-meshheading:3049938-Orthomyxoviridae,
pubmed-meshheading:3049938-Peptide Hydrolases,
pubmed-meshheading:3049938-Rats,
pubmed-meshheading:3049938-Receptors, Virus,
pubmed-meshheading:3049938-Viral Proteins,
pubmed-meshheading:3049938-Virus Cultivation
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pubmed:year |
1988
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pubmed:articleTitle |
Attachment of influenza C virus to human erythrocytes.
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pubmed:affiliation |
Department of Bacteriology, Yamagata University School of Medicine, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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