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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-23569

Hülsmeier, A J; Deplazes, P; Naem, S; Nonaka, N; Hennet, T; Köhler, P (2010). An Echinococcus multilocularis coproantigen is a surface glycoprotein with unique O-gycosylation. Glycobiology, 20(1):127-135.

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A major surface constituent of Echinococcus multilocularis adult worms, referred to as EmA9 antigen, was immunoaffinity purified and identified as a high molecular weight glycoconjugate. Labelling studies using the monoclonal antibody MAbEmA9 indicated that this antigen undergoes a regulated expression during the development from the larval to the adult parasite. Chemical modification of carbohydrate by periodate oxidation resulted in a reduced reactivity with antigen specific antibodies. Non-reductive beta-elimination of the purified molecule indicated the presence of O-linked glycans attached to threonine residues. Carbohydrate compositional analyses indicated the presence of N- and O-glycans with the ratio of carbohydrate to protein being 1.5:1 (w/w). N- and O-linked glycans were released by hydrazinolysis and analysed as 2-aminobenzamide derivatised glycans by mass spectrometry together with HPLC and enzymatic sequencing. Novel linear O-linked saccharides with multiple beta-HexNAc extensions of reducing end Gal were identified. N-linked glycans were also detected with oligomannose and mono-, bi-, tri- and tetra-antennary type structures, most of which were found to be core-fucosylated. Taken together, the results indicate that the EmA9 antigen is a glycoprotein located at the outer surface of the adult E. multilocularis. The observation that the EmA9 antigen expression is developmentally regulated suggests an involvement of this glycoprotein in the establishment of the parasite in its canine host.

Item Type:Journal Article, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Institute of Parasitology
04 Faculty of Medicine > Institute of Parasitology

04 Faculty of Medicine > Center for Integrative Human Physiology
04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology
DDC:570 Life sciences; biology
610 Medicine & health
600 Technology
Date:January 2010
Deposited On:01 Dec 2009 13:45
Last Modified:02 Dec 2013 17:40
Publisher:Oxford University Press
Funders:University of Zurich
Publisher DOI:10.1093/glycob/cwp155
PubMed ID:19822708
Citations:Web of Science®. Times Cited: 9
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Scopus®. Citation Count: 9

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