The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
A Scavenger Function for a DrosophilaPeptidoglycan Recognition Protein
Open accessAbstract
Recent studies of peptidoglycan recognition protein (PGRP) have shown that 2 of the 13 Drosophila PGRP genes encode proteins that function as receptors mediating immune responses to bacteria. We show here that another member, PGRP-SC1B, has a totally different function because it has enzymatic activity and thereby can degrade peptidoglycan. A mass spectrometric analysis of the cleavage products demonstrates that the enzyme hydrolyzes the lactylamide bond between the glycan strand and the cross-linking peptides. This result assigns the protein as an N-acetylmuramoyl-l-alanine amidase (EC ), and the corresponding gene is thus the first of this class to be described from a eukaryotic organism. Mutant forms of PGRP-SC1B lacking a potential zinc ligand are enzymatically inactive but retain their peptidoglycan affinity. The immunostimulatory properties of PGRP-SC1B-degraded peptidoglycan are much reduced. This is in striking contrast to lysozyme-digested peptidoglycan, which retains most of its elicitor activity. This points toward a scavenger function for PGRP-SC1B. Furthermore, a sequence homology comparison with phage T7 lysozyme, also an N-acetylmuramoyl-l-alanine amidase, shows that as many as six of the Drosophila PGRPs could belong to this class of proteins.
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Cited by
The immune response of Drosophila
Hoffmann, J. A. (2003) · Nature · doi:10.1038/nature02021 · Cited by 1,553
Immunity in Lepidopteran Insects
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Metadata
- Authors
- Mellroth, P., Karlsson, J., & Steiner, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-02
- Volume
- 278
- Issue
- 9
- Pages
- 7059-7064
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2006768051
- Cited by
- 342
- References
- 25
- FWCI
- 8.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
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