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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2007-12-31
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pubmed:abstractText |
Leishmania major culture-derived, soluble, exogenous antigens have been shown to be a source of vaccine targets for the parasite. We have previously reported that L. major culture-derived, soluble, exogenous antigens can immunize BALB/c mice against challenge with L. major. However, the molecule(s) involved in this protection was not known. We describe the potential of one component of soluble exogenous antigens (recombinant nucleoside hydrolase) to vaccinate mice against challenge with L. major. We found that recombinant nucleoside hydrolase vaccinated BALB/c mice against a subsequent challenge with L. major. Protection was manifested by a significant decrease in lesion size (as much as a 30-fold reduction) and parasite burden (as much as a 71-fold reduction). Protection was achieved whether recombinant nucleoside hydrolase was administered to mice in the presence or absence of adjuvant (interleukin-12). Finally, protection was accompanied by an increase in interferon-gamma production but a decrease in interleukin-10 production by vaccinated animals in response to challenge with L. major.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-10,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-12,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/N-Glycosyl Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Vaccines,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vaccines, Subunit
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0002-9637
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
77
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1060-5
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:18165522-Animals,
pubmed-meshheading:18165522-Antigens, Protozoan,
pubmed-meshheading:18165522-Female,
pubmed-meshheading:18165522-Interferon-gamma,
pubmed-meshheading:18165522-Interleukin-10,
pubmed-meshheading:18165522-Interleukin-12,
pubmed-meshheading:18165522-Interleukin-4,
pubmed-meshheading:18165522-Leishmania major,
pubmed-meshheading:18165522-Leishmaniasis, Cutaneous,
pubmed-meshheading:18165522-Lipopolysaccharides,
pubmed-meshheading:18165522-Mice,
pubmed-meshheading:18165522-Mice, Inbred BALB C,
pubmed-meshheading:18165522-N-Glycosyl Hydrolases,
pubmed-meshheading:18165522-Protozoan Vaccines,
pubmed-meshheading:18165522-Recombinant Proteins,
pubmed-meshheading:18165522-Time Factors,
pubmed-meshheading:18165522-Vaccination,
pubmed-meshheading:18165522-Vaccines, Subunit
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pubmed:year |
2007
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pubmed:articleTitle |
Protection of susceptible BALB/c mice from challenge with Leishmania major by nucleoside hydrolase, a soluble exo-antigen of Leishmania.
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pubmed:affiliation |
Department of Microbiology, Immunology, and Pathology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, CO 80523-1619, USA. malwabel@lamar.colostate.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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