rdf:type |
|
lifeskim:mentions |
umls-concept:C0019168,
umls-concept:C0019169,
umls-concept:C0026809,
umls-concept:C0042210,
umls-concept:C0449445,
umls-concept:C0871261,
umls-concept:C1513380,
umls-concept:C1521761,
umls-concept:C1627358,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2349975,
umls-concept:C2911692
|
pubmed:issue |
1
|
pubmed:dateCreated |
1996-11-26
|
pubmed:abstractText |
Mice were injected with immune complexes containing the recombinant hepatitis B surface antigen (HBsAg) vaccine (S + preS2) bound to different monoclonal antibodies (mAbs), in order to determine whether an enhancement of the response to a human vaccine could be obtained and observed. Enhancement and indifference were observed, as well as a decrease in immunogenicity. No relationship could be established between any effect and affinity or isotype of the bound mAbs. The preS2 region was rendered more immunogenic when an IgG2a mAb was bound to the S region of the HBsAg. The response to the S region was not modulated, whereas immunogenicity of the preS2 colinear region was decreased by antibody shielding. The mAb which was the most efficient as an enhancer of the antibody response also increased binding of the complexed immunogen to antigen presenting cells. The binding of a human mAb to the sole S region, but not to the preS2 region, should be tested as a potentiating agent of the anti-preS2 human immune response.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adjuvants, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigen-Antibody Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatitis B Surface Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatitis B Vaccines,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Isotypes
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0928-8244
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
13
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
71-9
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:8821401-Adjuvants, Immunologic,
pubmed-meshheading:8821401-Animals,
pubmed-meshheading:8821401-Antibodies, Bacterial,
pubmed-meshheading:8821401-Antibodies, Monoclonal,
pubmed-meshheading:8821401-Antibody Affinity,
pubmed-meshheading:8821401-Antibody Specificity,
pubmed-meshheading:8821401-Antigen-Antibody Complex,
pubmed-meshheading:8821401-Antigen-Presenting Cells,
pubmed-meshheading:8821401-Binding, Competitive,
pubmed-meshheading:8821401-Binding Sites, Antibody,
pubmed-meshheading:8821401-Epitopes,
pubmed-meshheading:8821401-Hepatitis B Surface Antigens,
pubmed-meshheading:8821401-Hepatitis B Vaccines,
pubmed-meshheading:8821401-Immunoglobulin Isotypes,
pubmed-meshheading:8821401-Mice
|
pubmed:year |
1996
|
pubmed:articleTitle |
Molecular analysis of the modulatory factors of the response to HBsAg in mice as an approach to HBV vaccine enhancement.
|
pubmed:affiliation |
Unité d'Immunologie Microbienne, Institut Pasteur, Paris, France.
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pubmed:publicationType |
Journal Article
|