Biochemical and ligand binding properties of recombinant Xenopus laevis cortical granule lectin-1

Intelectins are putative innate immune lectins that are found throughout chordates. The first intelectin reported was Xenopus laevis cortical granule lectin-1 (XCGL-1 or XL-35). XCGL-1 is critical in fertilization membrane development in Xenopus. Here, we explored the biochemical properties of XCGL-...

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Main Authors: Peerapon Deetanya, Thassanai Sitthiyotha, Nusara Chomanee, Surasak Chunsrivirot, Kittikhun Wangkanont
Format: Article
Language:English
Published: Elsevier 2022-08-01
Series:Heliyon
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S240584402201684X
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author Peerapon Deetanya
Thassanai Sitthiyotha
Nusara Chomanee
Surasak Chunsrivirot
Kittikhun Wangkanont
author_facet Peerapon Deetanya
Thassanai Sitthiyotha
Nusara Chomanee
Surasak Chunsrivirot
Kittikhun Wangkanont
author_sort Peerapon Deetanya
collection DOAJ
description Intelectins are putative innate immune lectins that are found throughout chordates. The first intelectin reported was Xenopus laevis cortical granule lectin-1 (XCGL-1 or XL-35). XCGL-1 is critical in fertilization membrane development in Xenopus. Here, we explored the biochemical properties of XCGL-1. The cysteines responsible for forming intermolecular disulfide bonds were identified. XCGL-1 adopted a four-lobed structure as observed by electron microscopy. The full-length XCGL-1 and the carbohydrate recognition domain (CRD) bind galactose-containing carbohydrates at nanomolar to micromolar affinities. Molecular modeling suggested that galactoside ligands coordinated the binding site calcium ion and interacted with residues around the groove made available by the non-conserved substitution compared to human intelectin-1. Folding conditions for production of recombinant XCGL-1 CRD were also investigated. Our results not only provide new biochemical insights into the function of XCGL-1, but may also provide foundation for further applications of XCGL-1 as glycobiology tools.
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spelling doaj.art-10e0365e1eca40969a5b3f9e002c53c62022-12-22T04:19:33ZengElsevierHeliyon2405-84402022-08-0188e10396Biochemical and ligand binding properties of recombinant Xenopus laevis cortical granule lectin-1Peerapon Deetanya0Thassanai Sitthiyotha1Nusara Chomanee2Surasak Chunsrivirot3Kittikhun Wangkanont4Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand; Center of Excellence for Molecular Crop, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, ThailandStructural and Computational Biology Research Unit, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, ThailandElectron Microscopy Unit, Department of Pathology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, 10700, ThailandStructural and Computational Biology Research Unit, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, ThailandCenter of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand; Center of Excellence for Molecular Crop, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand; Corresponding author.Intelectins are putative innate immune lectins that are found throughout chordates. The first intelectin reported was Xenopus laevis cortical granule lectin-1 (XCGL-1 or XL-35). XCGL-1 is critical in fertilization membrane development in Xenopus. Here, we explored the biochemical properties of XCGL-1. The cysteines responsible for forming intermolecular disulfide bonds were identified. XCGL-1 adopted a four-lobed structure as observed by electron microscopy. The full-length XCGL-1 and the carbohydrate recognition domain (CRD) bind galactose-containing carbohydrates at nanomolar to micromolar affinities. Molecular modeling suggested that galactoside ligands coordinated the binding site calcium ion and interacted with residues around the groove made available by the non-conserved substitution compared to human intelectin-1. Folding conditions for production of recombinant XCGL-1 CRD were also investigated. Our results not only provide new biochemical insights into the function of XCGL-1, but may also provide foundation for further applications of XCGL-1 as glycobiology tools.http://www.sciencedirect.com/science/article/pii/S240584402201684XXenopus laevis cortical granule lectin-1XCGL-1XL35IntelectinOmentin
spellingShingle Peerapon Deetanya
Thassanai Sitthiyotha
Nusara Chomanee
Surasak Chunsrivirot
Kittikhun Wangkanont
Biochemical and ligand binding properties of recombinant Xenopus laevis cortical granule lectin-1
Heliyon
Xenopus laevis cortical granule lectin-1
XCGL-1
XL35
Intelectin
Omentin
title Biochemical and ligand binding properties of recombinant Xenopus laevis cortical granule lectin-1
title_full Biochemical and ligand binding properties of recombinant Xenopus laevis cortical granule lectin-1
title_fullStr Biochemical and ligand binding properties of recombinant Xenopus laevis cortical granule lectin-1
title_full_unstemmed Biochemical and ligand binding properties of recombinant Xenopus laevis cortical granule lectin-1
title_short Biochemical and ligand binding properties of recombinant Xenopus laevis cortical granule lectin-1
title_sort biochemical and ligand binding properties of recombinant xenopus laevis cortical granule lectin 1
topic Xenopus laevis cortical granule lectin-1
XCGL-1
XL35
Intelectin
Omentin
url http://www.sciencedirect.com/science/article/pii/S240584402201684X
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