BOKU - Universität für Bodenkultur Wien - Forschungsinformationssystem

Logo BOKU-Forschungsportal

Gewählte Publikation:

Feng, C; Ghosh, A; Amin, MN; Giomarelli, B; Shridhar, S; Banerjee, A; Fernndez-Robledo, JA; Bianchet, MA; Wang, LX; Wilson, IB; Vasta, GR.
(2013): The galectin CvGal1 from the eastern oyster (Crassostrea virginica) binds to blood group A oligosaccharides on the hemocyte surface.
J Biol Chem. 2013; 288(34):24394-24409 FullText FullText_BOKU

Abstract:
The galectin CvGal1 from the eastern oyster (Crassostrea virginica), which possesses four tandemly arrayed carbohydrate recognition domains, was previously shown to display stronger binding to galactosamine and N-acetylgalactosamine relative to D-galactose. CvGal1 expressed by phagocytic cells is "hijacked" by the parasite Perkinsus marinus to enter the host, where it proliferates and causes systemic infection and death. In this study, a detailed glycan array analysis revealed that CvGal1 preferentially recognizes type 2 blood group A oligosaccharides. Homology modeling of the protein and its oligosaccharide ligands supported this preference over type 1 blood group A and B oligosaccharides. The CvGal ligand models were further validated by binding, inhibition, and competitive binding studies of CvGal1 and ABH-specific monoclonal antibodies with intact and deglycosylated glycoproteins, hemocyte extracts, and intact hemocytes and by surface plasmon resonance analysis. A parallel glycomic study carried out on oyster hemocytes (Kurz, S., Jin, C., Hykollari, A., Gregorich, D., Giomarelli, B., Vasta, G. R., Wilson, I. B. H., and Paschinger, K. (2013) J. Biol. Chem. 288,) determined the structures of oligosaccharides recognized by CvGal1. Proteomic analysis of the hemocyte glycoproteins identified beta-integrin and dominin as CvGal1 "self"-ligands. Despite strong CvGal1 binding to P. marinus trophozoites, no binding of ABH blood group antibodies was observed. Thus, parasite glycans structurally distinct from the blood group A oligosaccharides on the hemocyte surface may function as potentially effective ligands for CvGal1. We hypothesize that carbohydrate-based mimicry resulting from the host/parasite co-evolution facilitates CvGal1-mediated cross-linking to beta-integrin, located on the hemocyte surface, leading to cell activation, phagocytosis, and host infection.
Autor*innen der BOKU Wien:
Wilson Iain B.H.
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
ABO Blood-Group System - chemistry
Animals -
Crassostrea - chemistry
Galectins - chemistry
Hemocytes - chemistry
Oligosaccharides - chemistry
Protein Binding -
Proteomics - methods



Altmetric:
© BOKU Wien Impressum