Molecular cloning and characterization of a short peptidoglycan recognition protein from silkwormBombyx mori
Autor: | C. Ye, Ming-Yue Zhan, Xiao-Qiang Yu, Pei-Jin Yang, Xiang-Jun Rao |
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Rok vydání: | 2017 |
Předmět: |
0106 biological sciences
0301 basic medicine Signal peptide Innate immune system biology fungi Pattern recognition receptor Prophenoloxidase Molecular cloning biology.organism_classification 01 natural sciences Bacterial cell structure 010602 entomology 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Biochemistry Bombyx mori Insect Science Genetics Peptidoglycan Molecular Biology |
Zdroj: | Insect Molecular Biology. 26:665-676 |
ISSN: | 0962-1075 |
DOI: | 10.1111/imb.12330 |
Popis: | Peptidoglycan is the major bacterial component recognized by the insect immune system. Peptidoglycan recognition proteins (PGRPs) are a family of pattern-recognition receptors that recognize peptidoglycans and modulate innate immune responses. Some PGRPs retain N-acetylmuramoyl-L-alanine amidase (Enzyme Commission number: 3.5.1.28) activity to hydrolyse bacterial peptidoglycans. Others have lost the enzymatic activity and work only as immune receptors. They are all important modulators for innate immunity. Here, we report the cloning and functional analysis of PGRP-S4, a short-form PGRP from the domesticated silkworm, Bombyx mori. The PGRP-S4 gene encodes a protein of 199 amino acids with a signal peptide and a PGRP domain. PGRP-S4 was expressed in the fat body, haemocytes and midgut. Its expression level was significantly induced by bacterial challenges in the midgut. The recombinant PGRP-S4 bound bacteria and different peptidoglycans. In addition, it inhibited bacterial growth and hydrolysed an Escherichia coli peptidoglycan in the presence of Zn2+ . Scanning electron microscopy showed that PGRP-S4 disrupted the bacterial cell surface. PGRP-S4 further increased prophenoloxidase activation caused by peptidoglycans. Taken together, our data suggest that B. mori PGRP-S4 has multiple functions in immunity. |
Databáze: | OpenAIRE |
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