Abstract:
:The family of peptidoglycan recognition proteins (PGRPs) is conserved from insects to mammals. Recently, Drosophila PGRP-SC1B was demonstrated to be an N-acetylmuramoyl-L-alanine amidase (NAMLAA), an enzyme that cleaves the lactylamide bond between muramic acid and the peptide chain in peptidoglycan (PGN). We now show an M x mPGRP-L mRNA to be expressed in the liver. The recombinant M x mPGRP-L protein has NAMLAA activity and degrades PGN from both Escherichia coli and Staphylococcus aureus; however, the Gram-positive PGN was a better substrate after lysozyme treatment. The activity of M x mPGRP-L was further analysed using Bordetella pertussis tracheal toxin as a substrate. Cleavage products were separated on HPLC and identified using mass spectrometry. From these results we conclude that M x mPGRP-L has activity and other properties identifying it as the NAMLAA protein present in mammalian sera.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Gelius E,Persson C,Karlsson J,Steiner Hdoi
10.1016/s0006-291x(03)01096-9subject
Has Abstractpub_date
2003-07-11 00:00:00pages
988-94issue
4eissn
0006-291Xissn
1090-2104pii
S0006291X03010969journal_volume
306pub_type
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