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

Abstract 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...

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Autores principales:	Nongnuch Singrang, Sirasit Laophetsakunchai, Bich Ngoc Tran, Paul T. Matsudaira, Anchalee Tassanakajon, Kittikhun Wangkanont
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3daf8350777c4876a653a2c216ac7285
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spelling	oai:doaj.org-article:3daf8350777c4876a653a2c216ac72852021-12-02T14:06:32ZBiochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon10.1038/s41598-021-82301-52045-2322https://doaj.org/article/3daf8350777c4876a653a2c216ac72852021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-82301-5https://doaj.org/toc/2045-2322Abstract 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 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.Nongnuch SingrangSirasit LaophetsakunchaiBich Ngoc TranPaul T. MatsudairaAnchalee TassanakajonKittikhun WangkanontNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nongnuch Singrang Sirasit Laophetsakunchai Bich Ngoc Tran Paul T. Matsudaira Anchalee Tassanakajon Kittikhun Wangkanont Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon
description	Abstract 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 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.
format	article
author	Nongnuch Singrang Sirasit Laophetsakunchai Bich Ngoc Tran Paul T. Matsudaira Anchalee Tassanakajon Kittikhun Wangkanont
author_facet	Nongnuch Singrang Sirasit Laophetsakunchai Bich Ngoc Tran Paul T. Matsudaira Anchalee Tassanakajon Kittikhun Wangkanont
author_sort	Nongnuch Singrang
title	Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon
title_short	Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon
title_full	Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon
title_fullStr	Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon
title_full_unstemmed	Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon
title_sort	biochemical and structural characterization of a recombinant fibrinogen-related lectin from penaeus monodon
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/3daf8350777c4876a653a2c216ac7285
work_keys_str_mv	AT nongnuchsingrang biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT sirasitlaophetsakunchai biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT bichngoctran biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT paultmatsudaira biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT anchaleetassanakajon biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT kittikhunwangkanont biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon
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Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon

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