Source:http://linkedlifedata.com/resource/pubmed/id/16670324
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
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| pubmed:dateCreated |
2006-5-3
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| pubmed:abstractText |
Protective host immune responses to anthrax infection in humans and animal models are characterized by the development of neutralizing Abs against the receptor-binding anthrax protective Ag (PA), which, together with the lethal factor (LF) protease, composes anthrax lethal toxin (LT). We now report that B cells, in turn, are targets for LT. Anthrax PA directly binds primary B cells, resulting in the LF-dependent cleavage of the MAPK kinases (MAPKKs) and disrupted signaling to downstream MAPK targets. Although not directly lethal to B cells, anthrax LT treatment causes severe B cell dysfunction, greatly reducing proliferative responses to IL-4-, anti-IgM-, and/or anti-CD40 stimulation. Moreover, B cells treated with anthrax LT in vitro or isolated from mice treated with anthrax LT in vivo have a markedly diminished capacity to proliferate and produce IgM in response to TLR-2 and TLR-4 ligands. The suppressive effects of anthrax LT on B cell function occur at picomolar concentrations in vitro and at sublethal doses in vivo. These results indicate that anthrax LT directly inhibits the function of B cells in vitro and in vivo, revealing a potential mechanism through which the pathogen could bypass protective immune responses.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
AIM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunosuppressive Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase...,
http://linkedlifedata.com/resource/pubmed/chemical/anthrax toxin
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| pubmed:status |
MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
0022-1767
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
176
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
6155-61
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:16670324-Animals,
pubmed-meshheading:16670324-Antigens, Bacterial,
pubmed-meshheading:16670324-B-Lymphocytes,
pubmed-meshheading:16670324-Bacillus anthracis,
pubmed-meshheading:16670324-Bacterial Toxins,
pubmed-meshheading:16670324-Cell Proliferation,
pubmed-meshheading:16670324-Cells, Cultured,
pubmed-meshheading:16670324-Growth Inhibitors,
pubmed-meshheading:16670324-Humans,
pubmed-meshheading:16670324-Immunoglobulin M,
pubmed-meshheading:16670324-Immunoglobulins,
pubmed-meshheading:16670324-Immunosuppressive Agents,
pubmed-meshheading:16670324-Lymphocyte Activation,
pubmed-meshheading:16670324-Mice,
pubmed-meshheading:16670324-Mice, Inbred BALB C,
pubmed-meshheading:16670324-Mitogen-Activated Protein Kinase Kinases,
pubmed-meshheading:16670324-Signal Transduction,
pubmed-meshheading:16670324-Virulence
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| pubmed:year |
2006
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| pubmed:articleTitle |
Anthrax lethal toxin has direct and potent inhibitory effects on B cell proliferation and immunoglobulin production.
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| pubmed:affiliation |
Division of Monoclonal Antibodies, Office of Biotechnology Products, Office of Pharmaceutical Science, Center for Drug Evaluation and Research, U.S. Food and Drug Administration, Bethesda, MD 20892, USA.
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| pubmed:publicationType |
Journal Article
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