A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-L-alanine amidase activity
A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-L-alanine amidase activity
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DOI：
10.1016/s0006-291x(03)01096-9
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发表时间：
2003-07-11
影响因子：
3.1
通讯作者：
Steiner, H
中科院分区：
文献类型：
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作者：
Gelius, E;Persson, C;Steiner, H
肽聚糖识别蛋白（PGRP）家族是从昆虫到哺乳动物的保守蛋白。最近，果蝇PGRP-SC 1B被证明是一种N-乙酰胞壁酰-L-丙氨酸酰胺酶（NAMLAA），一种切割胞壁酸和肽聚糖（PGN）中肽链之间的乳酰酰胺键的酶。我们现在显示M.mPGRP-L mRNA在肝脏中表达。重组M.mPGRP-L蛋白具有NAMLAA活性，可降解大肠杆菌和金黄色葡萄球菌的PGN，但溶菌酶处理后革兰氏阳性PGN为更好的底物。使用百日咳博德特氏菌气管毒素作为底物进一步分析M.mPGRP-L的活性。裂解产物在HPLC上分离并使用质谱法鉴定。根据这些结果，我们得出结论，M.mPGRP-L具有活性和其他特性，将其鉴定为哺乳动物血清中存在的NAMLAA蛋白。(C)2003 Elsevier Science（美国）。All rights reserved.
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.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 Bordelella 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. (C) 2003 Elsevier Science (USA). All rights reserved.