Source:http://linkedlifedata.com/resource/pubmed/id/15922395
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2005-6-27
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| pubmed:abstractText |
Some viruses display enhanced infection for Fc receptor (FcR)-positive cell types when complexed with virus-specific immunoglobulin (Ig). This process has been termed antibody-dependent enhancement of viral infection (ADE). We reasoned that the mechanism of ADE could be exploited and adapted to target alphavirus-based vectors to FcR-positive cell types. Towards this goal, recombinant Sindbis viruses were constructed that express 1 to 4 immunoglobulin-binding domains of protein L (PpL) as N-terminal extensions of the E2 glycoprotein. PpL is a bacterial protein that binds the variable region of antibody kappa light chains from a range of mammalian species. The recombinant viruses incorporated PpL/E2 fusion proteins into the virion structure and recapitulated the species-specific Ig-binding phenotypes of native PpL. Virions reacted with non-immune serum or purified IgG displayed enhanced binding and ADE for several species-matched FcR-positive murine and human cell lines. ADE required virus expression of a functional PpL Ig-binding domain, and appeared to be FcgammaR-mediated. Specifically, ADE did not occur with FcgammaR-negative cells, did not require active complement proteins, and did not occur on FcgammaR-positive murine cell lines when virions were bound by murine IgG-derived F(ab')2 fragments.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Variable Region,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin kappa-Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vaccines, Synthetic,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glycoprotein E2, Sindbis virus
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0042-6822
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
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| pubmed:volume |
338
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
9-21
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:15922395-Amino Acid Sequence,
pubmed-meshheading:15922395-Animals,
pubmed-meshheading:15922395-BALB 3T3 Cells,
pubmed-meshheading:15922395-Bacterial Proteins,
pubmed-meshheading:15922395-Binding Sites,
pubmed-meshheading:15922395-Cell Line,
pubmed-meshheading:15922395-Cricetinae,
pubmed-meshheading:15922395-Genetic Vectors,
pubmed-meshheading:15922395-Humans,
pubmed-meshheading:15922395-Immunoglobulin Variable Region,
pubmed-meshheading:15922395-Immunoglobulin kappa-Chains,
pubmed-meshheading:15922395-Mice,
pubmed-meshheading:15922395-Molecular Sequence Data,
pubmed-meshheading:15922395-Receptors, Fc,
pubmed-meshheading:15922395-Recombinant Fusion Proteins,
pubmed-meshheading:15922395-Sindbis Virus,
pubmed-meshheading:15922395-Vaccines, Synthetic,
pubmed-meshheading:15922395-Viral Envelope Proteins
|
| pubmed:year |
2005
|
| pubmed:articleTitle |
Targeting Sindbis virus-based vectors to Fc receptor-positive cell types.
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| pubmed:affiliation |
Department of Microbiology and Immunology, Center for Molecular and Tumor Virology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, USA.
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| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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