Source:http://linkedlifedata.com/resource/pubmed/id/17208195
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2007-2-26
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pubmed:abstractText |
Chemokines are small (8-12 kDa) effector proteins that potentiate leukocyte chemonavigation. Beyond this role, certain chemokines have direct antimicrobial activity against human pathogenic organisms; such molecules are termed kinocidins. The current investigation was designed to explore the structure-activity basis for direct microbicidal activity of kinocidins. Amino acid sequence and 3-dimensional analyses demonstrated these molecules to contain iterations of the conserved gamma-core motif found in broad classes of classical antimicrobial peptides. Representative CXC, CC and C cysteine-motif-group kinocidins were tested for antimicrobial activity versus human pathogenic bacteria and fungi. Results demonstrate that these molecules exert direct antimicrobial activity in vitro, including antibacterial activity of native IL-8 and MCP-1, and microbicidal activity of native IL-8. To define molecular determinants governing its antimicrobial activities, the IL-8 gamma-core (IL-8gamma) and alpha-helical (IL-8alpha) motifs were compared to native IL-8 for antimicrobial efficacy in vitro. Microbicidal activity recapitulating that of native IL-8 localized to the autonomous IL-8alpha motif in vitro, and demonstrated durable microbicidal activity in human blood and blood matrices ex vivo. These results offer new insights into the modular architecture, context-related deployment and function, and evolution of host defense molecules containing gamma-core motifs and microbicidal helices associated with antimicrobial activity.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokines,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-8,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1768
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
598-608
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pubmed:dateRevised |
2007-12-3
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pubmed:meshHeading |
pubmed-meshheading:17208195-Amino Acid Motifs,
pubmed-meshheading:17208195-Amino Acid Sequence,
pubmed-meshheading:17208195-Anti-Bacterial Agents,
pubmed-meshheading:17208195-Candida albicans,
pubmed-meshheading:17208195-Chemokines,
pubmed-meshheading:17208195-Circular Dichroism,
pubmed-meshheading:17208195-Colony Count, Microbial,
pubmed-meshheading:17208195-Conserved Sequence,
pubmed-meshheading:17208195-Cysteine,
pubmed-meshheading:17208195-Humans,
pubmed-meshheading:17208195-Hydrogen-Ion Concentration,
pubmed-meshheading:17208195-Interleukin-8,
pubmed-meshheading:17208195-Microbial Sensitivity Tests,
pubmed-meshheading:17208195-Models, Molecular,
pubmed-meshheading:17208195-Molecular Sequence Data,
pubmed-meshheading:17208195-Peptides,
pubmed-meshheading:17208195-Protein Structure, Secondary,
pubmed-meshheading:17208195-Protein Structure, Tertiary,
pubmed-meshheading:17208195-Recombinant Proteins,
pubmed-meshheading:17208195-Salmonella typhimurium,
pubmed-meshheading:17208195-Sequence Homology, Amino Acid,
pubmed-meshheading:17208195-Spectrophotometry,
pubmed-meshheading:17208195-Staphylococcus aureus,
pubmed-meshheading:17208195-Structure-Activity Relationship
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pubmed:year |
2007
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pubmed:articleTitle |
Structural correlates of antimicrobial efficacy in IL-8 and related human kinocidins.
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pubmed:affiliation |
Division of Infectious Diseases, LAC-Harbor UCLA Medical Center, Torrance, CA 90509, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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