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dc.contributor.authorKaneko, Takashi
dc.contributor.authorGoldman, William E.
dc.contributor.authorMellroth, Peter
dc.contributor.authorSteiner, Hakan
dc.contributor.authorFukase, Koichi
dc.contributor.authorKusumoto, Shoichi
dc.contributor.authorHarley, William
dc.contributor.authorFox, Alvin
dc.contributor.authorGolenbock, Douglas T.
dc.contributor.authorSilverman, Neal S.
dc.date2022-08-11T08:09:10.000
dc.date.accessioned2022-08-23T16:20:08Z
dc.date.available2022-08-23T16:20:08Z
dc.date.issued2004-05-15
dc.date.submitted2008-12-19
dc.identifier.citationImmunity. 2004 May;20(5):637-49.
dc.identifier.issn1074-7613 (Print)
dc.identifier.pmid15142531
dc.identifier.urihttp://hdl.handle.net/20.500.14038/35213
dc.description.abstractInsects depend solely upon innate immune responses to survive infection. These responses include the activation of extracellular protease cascades, leading to melanization and clotting, and intracellular signal transduction pathways inducing antimicrobial peptide gene expression. In Drosophila, the IMD pathway is required for antimicrobial gene expression in response to gram-negative bacteria. The exact molecular component(s) from these bacteria that activate the IMD pathway remain controversial. We found that highly purified LPS did not stimulate the IMD pathway. However, lipid A, the active portion of LPS in mammals, activated melanization in the silkworm Bombyx morii. On the other hand, the IMD pathway was remarkably sensitive to polymeric and monomeric gram-negative peptidoglycan. Recognition of peptidoglycan required the stem-peptide sequence specific to gram-negative peptidoglycan and the receptor PGRP-LC. Recognition of monomeric and polymeric peptidoglycan required different PGRP-LC splice isoforms, while lipid A recognition required an unidentified soluble factor in the hemolymph of Bombyx morii.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=15142531&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/S1074-7613(04)00104-9
dc.subjectAnimals
dc.subjectBlotting, Northern
dc.subjectBombyx
dc.subjectCarrier Proteins
dc.subjectDrosophila
dc.subjectDrosophila Proteins
dc.subjectGram-Negative Bacteria
dc.subjectLipid A
dc.subjectLipopolysaccharides
dc.subjectPeptidoglycan
dc.subjectPolymerase Chain Reaction
dc.subjectProtein Isoforms
dc.subjectSignal Transduction
dc.subjectImmunology and Infectious Disease
dc.titleMonomeric and polymeric gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway
dc.typeJournal Article
dc.source.journaltitleImmunity
dc.source.volume20
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/infdis_pp/5
dc.identifier.contextkey684316
html.description.abstract<p>Insects depend solely upon innate immune responses to survive infection. These responses include the activation of extracellular protease cascades, leading to melanization and clotting, and intracellular signal transduction pathways inducing antimicrobial peptide gene expression. In Drosophila, the IMD pathway is required for antimicrobial gene expression in response to gram-negative bacteria. The exact molecular component(s) from these bacteria that activate the IMD pathway remain controversial. We found that highly purified LPS did not stimulate the IMD pathway. However, lipid A, the active portion of LPS in mammals, activated melanization in the silkworm Bombyx morii. On the other hand, the IMD pathway was remarkably sensitive to polymeric and monomeric gram-negative peptidoglycan. Recognition of peptidoglycan required the stem-peptide sequence specific to gram-negative peptidoglycan and the receptor PGRP-LC. Recognition of monomeric and polymeric peptidoglycan required different PGRP-LC splice isoforms, while lipid A recognition required an unidentified soluble factor in the hemolymph of Bombyx morii.</p>
dc.identifier.submissionpathinfdis_pp/5
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.contributor.departmentDepartment of Medicine, Division of Infectious Diseases and Immunology
dc.source.pages637-49


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