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The zebrafish galectins Drgal1-L2 and Drgal3-L1 bind in vitro to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and reduce viral adhesion to fish epithelial cells

DRS at CSIR-National Institute of Oceanography

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Title The zebrafish galectins Drgal1-L2 and Drgal3-L1 bind in vitro to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and reduce viral adhesion to fish epithelial cells
 
Creator Nita-Lazar, M.
Mancini, J.
Feng, C.
Gonzalez-Montalban, N.
Ravindran, C.
Jackson, S.
Heras-Sanchez, A.D.L.
Giomarelli, B.
Ahmed, H.
Haslam, S.M.
Wu, G.
Dell, A.
Ammayappan, A.
Vakharia, V.N.
Vasta, G.R.
 
Subject AQUACULTURE::Diseases of Cultured Organisms
ICHTHYOLOGY::General
ICHTHYOLOGY::Physiology, biochemistry, biophysics
 
Description The infectious hematopoietic necrosis virus (IHNV; Rhabdoviridae, Novirhabdovirus) infects teleost fish, such as salmon and trout, and is responsible for significant losses in the aquaculture industry and in wild fish populations. Although IHNV enters the host through the skin at the base of the fins, the viral adhesion and entry mechanisms are not fully understood. In recent years, evidence has accumulated in support of the key roles played by protein-carbohydrate interactions between host lectins secreted to the extracellular space and virion envelope glycoproteins in modulating viral adhesion and infectivity. In this study, we assessed in vitro the potential role(s) of zebrafish (Danio rerio) proto type galectin-1 (Drgal1-L2) and a chimera galectin-3 (Drgal3-L1) in IHNV adhesion to epithelial cells. Our results suggest that the extracellular Drgal1-L2 and Drgal3-L1 interact directly and in a carbohydrate-dependent manner with the IHNV glycosylated envelope and glycans on the epithelial cell surface, significantly reducing viral adhesion
 
Date 2016-02-04T04:46:05Z
2016-02-04T04:46:05Z
2016
 
Type Journal Article
 
Identifier Developmental and Comparative Immunology, vol.55; 2016; 241-252
http://drs.nio.org/drs/handle/2264/4900
 
Language en
 
Rights An edited version of this paper was published by Elsevier. Copyright [2015] Elsevier
 
Publisher Elsevier