Document Detail


Cleavage of PGRP-LC receptor in the Drosophila IMD pathway in response to live bacterial infection in S2 cells.
MedLine Citation:
PMID:  22496930     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Drosophila responds to Gram-negative bacterial infection by activating the immune deficiency (IMD) pathway, leading to production of antimicrobial peptides (AMPs). As a receptor for the IMD pathway, peptidoglycan-recognition protein (PGRP), PGRP-LC is known to recognize and bind monomeric peptidoglycan (DAP-type PGN) through its PGRP ectodomain and in turn activate the IMD pathway. The questions remain how PGRP-LC is activated in response to pathogen infection to initiate the IMD signal transduction in Drosophila. Here we present evidence to show that proteases such as elastase and Mmp2 can also activate the IMD pathway but not the TOLL pathway. The elastase-dependent IMD activation requires the receptor PGRP-LC. Importantly, we find that live Salmonella/E. coli infection modulates PGRP-LC expression/receptor integrity and activates the IMD pathway while dead Salmonella/E. coli or protease-deficient E. coli do neither. Our results suggest an interesting possibility that Gram-negative pathogen infection may be partially monitored through the structural integrity of the receptor PGRP-LC via an infection-induced enzyme-based cleavage-mediated activation mechanism.
Authors:
Rebecca L Schmidt; Francesca M Rinaldo; Shayla E Hesse; Masakazu Hamada; Zachary Ortiz; Daniah T Beleford; Andrea Page-McCaw; Jeffrey L Platt; Amy H Tang
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-7-1
Journal Detail:
Title:  Self/nonself     Volume:  2     ISSN:  1938-2049     ISO Abbreviation:  -     Publication Date:  2011 7 
Date Detail:
Created Date:  2012-4-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101495364     Medline TA:  Self Nonself     Country:  -    
Other Details:
Languages:  ENG     Pagination:  125-141     Citation Subset:  -    
Affiliation:
Department of Biochemistry and Molecular Biology; Mayo Clinic Cancer Center; Mayo Clinic College of Medicine; Rochester, MN USA.
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