Linked Life Data

16303095

Source:http://linkedlifedata.com/resource/pubmed/id/16303095

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2005-11-23
pubmed:abstractText
The structural requirements for recognition of peptidoglycan (PGN) by PGRP-LC and activation of the Drosophila IMD pathway are not yet clear. In order to examine this question more carefully, the activity of peptidoglycan from different types of bacteria was compared in cell-based and whole animal assays. Drosophila S2* cells, but not adult flies, responded to Lys-type Micrococcus luteus PGN, but with significantly less potency compared to Dap-type Escherichia coli PGN, while intact Lys-type PGN from Staphylococcus aureus was inactive. After treatment with lysostaphin, which digests the cross-bridging peptides, S. aureus PGN weakly stimulated the IMD pathway, similar to M. luteus PGN. Further digestion with mutanolysin, which creates monomeric PGN fragments, abolished the activity of S. aureus PGN. On the other hand, monomeric E. coli PGN, generated by mutanolysin digestion, was still active but required different isoforms of PGRP-LC for recognition. Polymeric PGN required only PGRP-LCx, while monomeric E. coli PGN required both the PGRP-LCa and PGRP-LCx isoforms. These results suggest that the recognition by PGRP-LCx alone requires polymeric PGN, and that polymeric Dap-type PGN is a more potent PGRP-LCx agonist, compared to Lys-type PGN. These results also suggest that the heteromeric PGRP-LCa/LCx receptor complex recognizes monomeric Dap-type, but not Lys-type, PGN.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0968-0519
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
383-9
pubmed:dateRevised
2010-12-28
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Peptidoglycan recognition by the Drosophila Imd pathway.
pubmed:affiliation
Division of Infectious Diseases, Department of Medicine, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, N.I.H., Extramural