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Reference Report
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| Citation | Mellroth, P., Karlsson, J., Steiner, H. (2003). A scavenger function for a Drosophila peptidoglycan recognition protein. J. Biol. Chem. 278(9): 7059--7064. (Export to RIS) | ||
| FlyBase ID | FBrf0159028 | ||
| Publication Type | Research paper | ||
| PubMed ID | 12496260 | ||
| PubMed Abstract | 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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| Language of Publication | English | ||
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| Publication Type | Journal | ||
| Abbreviation | J. Biol. Chem. | ||
| Title | Journal of Biological Chemistry | ||
| Publication Year | 1905- | ||
| ISBN/ISSN | 0021-9258 | ||
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Data from Reference
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| Alleles (4)
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| Genes (9)
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