Source:http://linkedlifedata.com/resource/pubmed/id/15806982
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-4-5
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pubmed:abstractText |
Gastric colonization of Helicobacter pylori (H. pylori) occurs in a very early age via infected mothers having H. pylori-specific IgG antibodies that would be transplacentally transferred to infants. In addition, H. pylori urease-specific IgG was associated with chronic gastric atrophy and post-immunization gastritis is usually correlated with a strong local IgG response. These findings indicate that H. pylori-specific IgG antibodies, in particular its urease-specific IgG, may induce unfavorable influence on host resistance against H. pylori. Here, we show that we have found a unique H. pylori urease-specific IgG monoclonal antibody (MAb), termed S3, recognizing the conformational structure of the small subunit Ure-A, which enhanced the urease enzymatic activity. Such enhancement of the H. pylori urease activity induced by 1 microg of S3 was almost completely cancelled by simultaneously added the same amount of L2 MAb, which has a strong and specific inhibitory activity against H. pylori urease and recognizes a liner epitope of 8-mer peptide (F8: SIKEDVQF) within its large subunit Ure-B (Infect. Immun. 69: 6597, 2001). Intravenous pre-administration of purified S3 into BALB/c mice showed significant augmentation for gastric colonization with the susceptible strain Sydney Strain-1 (SS-1). To our knowledge, this is the first demonstration that a H. pylori urease-specific IgG MAb induced an augmentation of their gastric colonization in vivo.
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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, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Urease
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0388-6107
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35-42
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15806982-Amino Acid Sequence,
pubmed-meshheading:15806982-Animals,
pubmed-meshheading:15806982-Antibodies, Bacterial,
pubmed-meshheading:15806982-Antibodies, Monoclonal,
pubmed-meshheading:15806982-Antibody Specificity,
pubmed-meshheading:15806982-Antigens, Bacterial,
pubmed-meshheading:15806982-Epitope Mapping,
pubmed-meshheading:15806982-Female,
pubmed-meshheading:15806982-Gastric Mucosa,
pubmed-meshheading:15806982-Gastritis,
pubmed-meshheading:15806982-Helicobacter Infections,
pubmed-meshheading:15806982-Helicobacter pylori,
pubmed-meshheading:15806982-Immunoglobulin G,
pubmed-meshheading:15806982-Mice,
pubmed-meshheading:15806982-Mice, Inbred BALB C,
pubmed-meshheading:15806982-Molecular Sequence Data,
pubmed-meshheading:15806982-Urease
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pubmed:year |
2005
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pubmed:articleTitle |
Augmentation of Helicobacter pylori urease activity by its specific IgG antibody: implications for bacterial colonization enhancement.
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pubmed:affiliation |
Department of Microbiology and Immunology, Third Department of Internal Medicine, Nippon Medical School, Tokyo 113-8602, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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