15556270

Source:http://linkedlifedata.com/resource/pubmed/id/15556270

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0013138, umls-concept:C0205373, umls-concept:C0301872, umls-concept:C0936012
pubmed:issue	9-10
pubmed:dateCreated	2004-11-23
pubmed:abstractText	Insects have developed an efficient host defense against microorganisms, which involves humoral and cellular mechanisms. Numerous data highlight similarities between defense responses of insects and innate immunity of mammals. The fruit fly, Drosophila melanogaster, is a favorable model system for the analysis of the first line defense against microorganisms. Taking advantages of improvements in mass spectrometry (MS), two-dimensional (2D) gel electrophoresis and bioinformatics, differential analyses of blood content (hemolymph) from immune-challenged versus control Drosophila were performed. Two strategies were developed: (i) peptidomic analyses through matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) MS and high performance liquid chromatography for molecules below 15 kDa, and (ii) proteomic studies based on 2D gel electrophoresis, MALDI-TOF fingerprinting and database searches, for compounds of greater molecular masses. The peptidomic strategy led to the detection of a large number of peptides induced in the hemolymph of challenged flies as compared to controls. Of these, 28 were characterized, amongst which were antimicrobial peptides. The 2D gel electrophoresis strategy led to the detection of 70 spots differentially regulated by at least fivefold after microbial infection. This approach yielded the identity of a series of proteins that were related to the Drosophila immune response, such as proteases, protease inhibitors, prophenoloxydase-activating enzymes, serpins and a Gram-negative binding protein-like protein. This strategy also brought to light new candidates with a potential function in the immune response (odorant-binding protein, peptidylglycine alpha-hydroxylating monooxygenase and transferrin). Interestingly, several molecules resulting from the cleavage of proteins were detected after a fungal infection. Together, peptidomic and proteomic analyses represent new tools to characterize molecules involved in the innate immune reactions of Drosophila.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/1264604
pubmed:citationSubset	IM
pubmed:status	MEDLINE
pubmed:issn	0300-9084
pubmed:author	pubmed-author:BuletPhilippeP, pubmed-author:CharletMauriceM, pubmed-author:Ehret-SabatierLaurenceL, pubmed-author:HoffmannJules AJA, pubmed-author:LevyFrancineF, pubmed-author:RabelDavidD
pubmed:issnType	Print
pubmed:volume	86
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	607-16
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:15556270-Animals, pubmed-meshheading:15556270-Drosophila, pubmed-meshheading:15556270-Immunity, pubmed-meshheading:15556270-Proteomics
pubmed:articleTitle	Peptidomic and proteomic analyses of the systemic immune response of Drosophila.
pubmed:affiliation	Institut de Biologie Moléculaire et Cellulaire, 15 rue René Descartes, 67084 Strasbourg cedex, France.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't