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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1999-5-7
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pubmed:abstractText |
BBG2Na is a protein comprising residues 130-230 of the respiratory syncytial virus subgroup A (RSV-A) G protein (G2Na) fused to the albumin-binding domain of streptococcal G protein (BB). BBG2Na was cloned, expressed in Escherichia coli and renaturated. In rodent models, this subunit RSV vaccine adjuvanted in Alhydrogel induced specific antibodies and conferred protection to RSV infection. Comparison of the antibody production in a BALB/c mouse model revealed that BBG2Na induced a stronger and earlier G2Na antibody response than G2Na alone, without altering the IgG subclass distribution. To address the role of the BB part, we explored its carrier properties and showed that it is a Th dependent antigen, generating a more potent G2Na-specific B cell memory response and able to generate Th cells that provide help for G2Na antibody production.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HN Protein,
http://linkedlifedata.com/resource/pubmed/chemical/IgG Fc-binding protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin,
http://linkedlifedata.com/resource/pubmed/chemical/Vaccines, Synthetic,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Vaccines,
http://linkedlifedata.com/resource/pubmed/chemical/attachment protein G
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0264-410X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
406-14
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:10073717-Animals,
pubmed-meshheading:10073717-Antibodies, Viral,
pubmed-meshheading:10073717-Antigens, Bacterial,
pubmed-meshheading:10073717-Bacterial Proteins,
pubmed-meshheading:10073717-Female,
pubmed-meshheading:10073717-HN Protein,
pubmed-meshheading:10073717-Immunoglobulin G,
pubmed-meshheading:10073717-Mice,
pubmed-meshheading:10073717-Mice, Inbred BALB C,
pubmed-meshheading:10073717-Peptide Fragments,
pubmed-meshheading:10073717-Respiratory Syncytial Viruses,
pubmed-meshheading:10073717-Serum Albumin,
pubmed-meshheading:10073717-Vaccines, Synthetic,
pubmed-meshheading:10073717-Viral Envelope Proteins,
pubmed-meshheading:10073717-Viral Proteins,
pubmed-meshheading:10073717-Viral Vaccines
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pubmed:year |
1999
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pubmed:articleTitle |
The serum albumin-binding region of streptococcal protein G (BB) potentiates the immunogenicity of the G130-230 RSV-A protein.
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pubmed:affiliation |
Centre d'Immunologie, Inst. de Recherche Pierre Fabre, Saint-Julien-en-Genevois, France. christine.libon@pierre-fabre.com
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pubmed:publicationType |
Journal Article
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