Literature DB >> 21945438

Lectin activity of the nucleocytoplasmic EUL protein from Arabidopsis thaliana.

Jonas Van Hove1, Elke Fouquaert, David F Smith, Paul Proost, Els J M Van Damme.   

Abstract

The Euonymus lectin (EUL) domain was recognized as the structural motif for a novel class of putative carbohydrate binding proteins. Confocal microscopy demonstrated that the lectin from Euonymus europaeus (EEA) as well as the EUL protein from Arabidopsis thaliana (ArathEULS3) are located in the nucleocytoplasmic compartment of the plant cell. ArathEULS3 as well as its EUL domain were successfully expressed in Pichia pastoris and purified. The EUL domain from Arabidopsis interacts with glycan structures containing Lewis Y, Lewis X and lactosamine, indicating that it can be considered a true lectin domain. Despite the high sequence identity between the EUL domains in EEA and ArathEULS3, both domains recognize different carbohydrate structures.
Copyright © 2011 Elsevier Inc. All rights reserved.

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Year:  2011        PMID: 21945438      PMCID: PMC3195871          DOI: 10.1016/j.bbrc.2011.09.031

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  20 in total

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Journal:  Science       Date:  2002-03-21       Impact factor: 47.728

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  12 in total

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2.  Arabidopsis F-box protein containing a Nictaba-related lectin domain interacts with N-acetyllactosamine structures.

Authors:  Karolina Stefanowicz; Nausicaä Lannoo; Paul Proost; Els J M Van Damme
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Review 4.  Role of Protein Glycosylation in Host-Pathogen Interaction.

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10.  High-Mannose Specific Lectin and Its Recombinants from a Carrageenophyta Kappaphycus alvarezii Represent a Potent Anti-HIV Activity Through High-Affinity Binding to the Viral Envelope Glycoprotein gp120.

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Journal:  Mar Biotechnol (NY)       Date:  2015-11-23       Impact factor: 3.619

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