Source:http://linkedlifedata.com/resource/pubmed/id/16734561
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
2006-5-31
|
| pubmed:abstractText |
Human and mouse genomes contain more than 20 related genes encoding diverse type I interferons (IFNs- alpha/beta), cytokines that are crucial for resistance of organisms against viral infections. Although the amino acid sequences of various IFN-alpha/beta subtypes differ markedly, they are all considered to share a common three-dimensional structure and to bind the same heterodimeric receptor, composed of the IFNAR-1 and IFNAR-2 subunits. Analysis of available mammalian IFN-beta sequences showed that they all carry 1 to 5 predicted N-glycosylation sites. Murine IFN-beta contains three predicted N-glycosylation sites (Asn29, Asn69, Asn76), one of which (Asn29) is located in the AB loop, in a region predicted to interact with the type I IFN receptor. The aim of this work was to test if this site is indeed N-glycosylated and if this glycosylation would affect IFN antiviral activity. We showed that all three N-glycosylation sites predicted from the sequence, including Asn29, carry N-linked sugars. Mutation of individual N-glycosylation sites had a weak negative influence on IFN antiviral activity. In contrast, the complete loss of glycosylation dramatically decreased activity. Our data suggest that interaction of murine IFN-beta with the IFNAR could locally differ from that of human IFN-alpha2 and human IFN-beta.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/IFNAR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ifnar2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-beta,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Interferon alpha-beta,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interferon
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
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| pubmed:issn |
1079-9907
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
26
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
406-13
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:16734561-3T3 Cells,
pubmed-meshheading:16734561-Amino Acid Sequence,
pubmed-meshheading:16734561-Amino Acid Substitution,
pubmed-meshheading:16734561-Animals,
pubmed-meshheading:16734561-Aspartic Acid,
pubmed-meshheading:16734561-Binding Sites,
pubmed-meshheading:16734561-Cell Line,
pubmed-meshheading:16734561-Glycosylation,
pubmed-meshheading:16734561-Humans,
pubmed-meshheading:16734561-Interferon-beta,
pubmed-meshheading:16734561-Membrane Proteins,
pubmed-meshheading:16734561-Mice,
pubmed-meshheading:16734561-Mice, Inbred BALB C,
pubmed-meshheading:16734561-Models, Molecular,
pubmed-meshheading:16734561-Molecular Sequence Data,
pubmed-meshheading:16734561-Protein Binding,
pubmed-meshheading:16734561-Protein Conformation,
pubmed-meshheading:16734561-Protein Structure, Secondary,
pubmed-meshheading:16734561-Receptor, Interferon alpha-beta,
pubmed-meshheading:16734561-Receptors, Interferon,
pubmed-meshheading:16734561-Sequence Homology, Amino Acid
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| pubmed:year |
2006
|
| pubmed:articleTitle |
N-glycosylation of murine IFN-beta in a putative receptor-binding region.
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| pubmed:affiliation |
Université Catholique de Louvain, Christian de Duve Institute of Cellular Pathology, Microbial Pathogenesis Unit, B-1200, Brussels, Belgium.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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