ArticlePLoS biology2004
A Drosophila pattern recognition receptor contains a peptidoglycan docking groove and unusual L,D-carboxypeptidase activity.
Article in PLoS biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 111 citations in OpenAlex.
- RfGNBP5 Negatively Regulates Innate Immunity of Red Palm Weevil,Microorganisms · 2026Article
- The Gut Microbiota ofMicroorganisms · 2025Review
- Molecular and Functional Characterization of a Short-Type Peptidoglycan Recognition Protein, Ct-PGRP-S1 in the Giant Triton SnailInternational journal of molecular sciences · 2022Article
- Preferential binding of DAP-PGs by major peptidoglycan recognition proteins found in cell-free hemolymph of Manduca sexta.Insect biochemistry and molecular biology · 2022Article
- Sensing microbial infections in the Drosophila melanogaster genetic model organism.Immunogenetics · 2022Review
- Bacterial recognition by PGRP-SA and downstream signalling by Toll/DIF sustain commensal gut bacteria in Drosophila.PLoS genetics · 2022Article
- PGRP-LB: An Inside View into the Mechanism of the Amidase Reaction.International journal of molecular sciences · 2021Article
- Parasite Presence Induces Gene Expression Changes in an Ant Host Related to Immunity and Longevity.Genes · 2021Article
- Structural and Functional Analysis of PGRP-LC Indicates Exclusive Dap-Type PGN Binding in Bumblebees.International journal of molecular sciences · 2020Article
- Article
- Antimicrobial peptides fromRSC advances · 2019Review
- Accessibility to Peptidoglycan Is Important for the Recognition of Gram-Positive Bacteria in Drosophila.Cell reports · 2019Article
- The three-dimensional structure and recognition mechanism of Manduca sexta peptidoglycan recognition protein-1.Insect biochemistry and molecular biology · 2019Article
- Dehydration triggers ecdysone-mediated recognition-protein priming and elevated anti-bacterial immune responses in Drosophila Malpighian tubule renal cells.BMC biology · 2018Article
- Crystal structure of peptidoglycan recognition protein SA in Apis mellifera (Hymenoptera: Apidae).Protein science : a publication of the Protein Society · 2018Article
- PGRP-LD mediates A. stephensi vector competency by regulating homeostasis of microbiota-induced peritrophic matrix synthesis.PLoS pathogens · 2018Article
- Orthologous and Paralogous AmpD Peptidoglycan Amidases from Gram-Negative Bacteria.Microbial drug resistance (Larchmont, N.Y.) · 2016Review
- Staphylococcus aureus Survives with a Minimal Peptidoglycan Synthesis Machine but Sacrifices Virulence and Antibiotic Resistance.PLoS pathogens · 2015Article
- Bacterial and fungal pattern recognition receptors in homologous innate signaling pathways of insects and mammals.Frontiers in microbiology · 2015Review
- Molecular cloning and mRNA expression of the peptidoglycan recognition protein gene HcPGRP1 and its isoform HcPGRP1a from the freshwater mussel Hyriopsis cumingi.Genetics and molecular biology · 2014Article
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Authors and funding
8 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Drosophila peptidoglycan recognition protein SA (PGRP-SA) is critically involved in sensing bacterial infection and activating the Toll signaling pathway, which induces the expression of specific antimicrobial peptide genes. We have determined the crystal structure of PGRP-SA to 2.2-A resolution and analyzed its peptidoglycan (PG) recognition and signaling activities. We found an extended surface groove in the structure of PGRP-SA, lined with residues that are highly diverse among different PGRPs. Mutational analysis identified it as a PG docking groove required for Toll signaling and showed that residue Ser158 is essential for both PG binding and Toll activation. Contrary to the general belief that PGRP-SA has lost enzyme function and serves primarily for PG sensing, we found that it possesses an intrinsic L,D-carboxypeptidase activity for diaminopimelic acid-type tetrapeptide PG fragments but not lysine-type PG fragments, and that Ser158 and His42 may participate in the hydrolytic activity. As L,D-configured peptide bonds exist only in prokaryotes, this work reveals a rare enzymatic activity in a eukaryotic protein known for sensing bacteria and provides a possible explanation of how PGRP-SA mediates Toll activation specifically in response to lysine-type PG.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.