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Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon

by Tran, Bich Ngoc , Tassanakajon, Anchalee , Singrang, Nongnuch , Laophetsakunchai, Sirasit , Matsudaira, Paul T. , Wangkanont, Kittikhun

in 631/250/262 / 631/45/221 / 631/45/535 / 631/45/612 / Adaptive immunity / Agglutination / Biological activity / Calcium / Crustaceans / Economic importance / Electron microscopy / Fibrinogen / Humanities and Social Sciences / Immune clearance / Immune system / Infectious diseases / Innate immunity / Invertebrates / Lectins / multidisciplinary / Penaeus monodon / Science / Science (multidisciplinary)

2021

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Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon

by Tran, Bich Ngoc , Tassanakajon, Anchalee , Singrang, Nongnuch , Laophetsakunchai, Sirasit , Matsudaira, Paul T. , Wangkanont, Kittikhun

2021

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Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon

by Tran, Bich Ngoc , Tassanakajon, Anchalee , Singrang, Nongnuch , Laophetsakunchai, Sirasit , Matsudaira, Paul T. , Wangkanont, Kittikhun

2021

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Journal Article

Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon

Tran, Bich Ngoc,

Tassanakajon, Anchalee,

Singrang, Nongnuch,

Laophetsakunchai, Sirasit,

Matsudaira, Paul T.,

Wangkanont, Kittikhun

2021

Overview

Fibrinogen-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 Pm FREP from the black tiger shrimp Penaeus monodon expressed in the Trichoplusia ni insect cell. Electron microscopy and cross-linking experiments revealed that Pm FREP is a disulfide-linked dimer of pentamers distinct from other fibrinogen-related lectins. The full-length protein binds N-acetyl sugars in a Ca 2+ ion-independent manner. Pm FREP recognized and agglutinated Pseudomonas aeruginosa . Weak binding was detected with other bacteria, including Vibrio parahaemolyticus , but no agglutination activity was observed. The biologically active Pm FREP 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.

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Publisher

Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio

Subject

/ Biological activity