A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-L-alanine amidase activity
2003 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, Vol. 306, no 4, 988-994 p.Article in journal (Refereed) Published
The family of peptidoglycan recognition proteins (PGRPs) is conserved from insects to mammals. Recently, Drosophila PGRP-SC1B was demonstrated to be an N-acetylmuramoyl- -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.mPGRP-L mRNA to be expressed in the liver. The recombinant M.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.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.mPGRP-L has activity and other properties identifying it as the NAMLAA protein present in mammalian sera.
Place, publisher, year, edition, pages
2003. Vol. 306, no 4, 988-994 p.
IdentifiersURN: urn:nbn:se:su:diva-20035DOI: 10.1016/S0006-291X(03)01096-9PubMedID: 12821140OAI: oai:DiVA.org:su-20035DiVA: diva2:186560