6E20

Crystal structure of the Dario rerio galectin-1-L2

6E20 の概要

• エントリーDOI: 10.2210/pdb6e20/pdb
• 関連するPDBエントリー: 1GAN
• 関連するBIRD辞書のPRD_ID: PRD_900019
• 分子名称: Galectin, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: galectin-1, innate immunity infectious hematopoietic necrosis virus (ihnv), danio rerio, zebrafish, sugar binding protein
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31657.78

構造登録者

Ghosh, A.,Bianchet, M.A. (登録日: 2018-07-10, 公開日: 2019-03-20, 最終更新日: 2023-10-11)

主引用文献

Ghosh, A.,Banerjee, A.,Amzel, L.M.,Vasta, G.R.,Bianchet, M.A.
Structure of the zebrafish galectin-1-L2 and model of its interaction with the infectious hematopoietic necrosis virus (IHNV) envelope glycoprotein.
Glycobiology, 29:419-430, 2019

PubMed Abstract: Galectins, highly conserved β-galactoside-binding lectins, have diverse regulatory roles in development and immune homeostasis and can mediate protective functions during microbial infection. In recent years, the role of galectins in viral infection has generated considerable interest. Studies on highly pathogenic viruses have provided invaluable insight into the participation of galectins in various stages of viral infection, including attachment and entry. Detailed mechanistic and structural aspects of these processes remain undetermined. To address some of these gaps in knowledge, we used Zebrafish as a model system to examine the role of galectins in infection by infectious hematopoietic necrosis virus (IHNV), a rhabdovirus that is responsible for significant losses in both farmed and wild salmonid fish. Like other rhabdoviruses, IHNV is characterized by an envelope consisting of trimers of a glycoprotein that display multiple N-linked oligosaccharides and play an integral role in viral infection by mediating the virus attachment and fusion. Zebrafish's proto-typical galectin Drgal1-L2 and the chimeric-type galectin Drgal3-L1 interact directly with the glycosylated envelope of IHNV, and significantly reduce viral attachment. In this study, we report the structure of the complex of Drgal1-L2 with N-acetyl-d-lactosamine at 2.0 Å resolution. To gain structural insight into the inhibitory effect of these galectins on IHNV attachment to the zebrafish epithelial cells, we modeled Drgal3-L1 based on human galectin-3, as well as, the ectodomain of the IHNV glycoprotein. These models suggest mechanisms for which the binding of these galectins to the IHNV glycoprotein hinders with different potencies the viral attachment required for infection.

PubMed: 30834446
DOI: 10.1093/glycob/cwz015

実験手法

X-RAY DIFFRACTION (2 Å)