Author:
Singrang Nongnuch,Laophetsakunchai Sirasit,Tran Bich Ngoc,Matsudaira Paul T.,Tassanakajon Anchalee,Wangkanont Kittikhun
Abstract
AbstractFibrinogen-related lectins are carbohydrate-binding proteins of the innate immune system that recognize glycan structures on microbial surfaces. These innate immune lectins are crucial for invertebrates as they do not rely on adaptive immunity for pathogen clearance. Here, we characterize a recombinant fibrinogen-related lectin PmFREP from the black tiger shrimp Penaeus monodon expressed in the Trichoplusia ni insect cell. Electron microscopy and cross-linking experiments revealed that PmFREP is a disulfide-linked dimer of pentamers distinct from other fibrinogen-related lectins. The full-length protein binds N-acetyl sugars in a Ca2+ ion-independent manner. PmFREP recognized and agglutinated Pseudomonas aeruginosa. Weak binding was detected with other bacteria, including Vibrio parahaemolyticus, but no agglutination activity was observed. The biologically active PmFREP will not only be a crucial tool to elucidate the innate immune signaling in P. monodon and other economically important species, but will also aid in detection and prevention of shrimp bacterial infectious diseases.
Funder
Chulalongkorn University grant to the Center of Excellence for Molecular Biology and Genomics of Shrimp
Chulalongkorn University grant to the Molecular Crop Research Unit
Second Century Fund (C2F), Chulalongkorn University
Thailand Research Fund and Office of the Higher Education Commission, Ministry of Education Research Grant for New Scholar
Publisher
Springer Science and Business Media LLC
Cited by
6 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献