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Isomeric separation and recognition of anionic and zwitterionic n-glycans from royal jelly glycoproteins

Journal article
Authors A. Hykollari
D. Malzl
B. Eckmair
J. Vanbeselaere
P. Scheidl
Chunsheng Jin
Niclas G. Karlsson
I. B. H. Wilson
K. Paschinger
Published in Molecular and Cellular Proteomics
Volume 17
Issue 11
Pages 2177-2196
ISSN 1535-9476
Publication year 2018
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 2177-2196
Language en
Links dx.doi.org/10.1074/mcp.RA117.000462
Subject categories Cell and Molecular Biology

Abstract

Royal jelly has received attention because of its necessity for the development of queen honeybees as well as claims of benefits on human health; this product of the hypopharyngeal glands of worker bees contains a large number of proteins, some of which have been claimed to have various biological effects only in their glycosylated state. However, although there have been glycomic and glycoproteomic analyses in the past, none of the glycan structures previously defined would appear to have potential to trigger specific biological functions. In the current study, whole royal jelly as well as single protein bands were subject to off-line LC-MALDI-TOF MS glycomic analyses, complemented by permethylation, Western blotting and arraying data. Similarly to recent in-depth studies on other insect species, previously overlooked glucuronic acid termini, sulfation of mannose residues and core β-mannosylation of the N-glycans were found; additionally, a relatively rare zwitterionic modification with phosphoethanolamine is present, in contrast to the phosphorylcholine occurring in lepidopteran species. Indicative of tissue-specific remodelling of glycans in the Golgi apparatus of hypopharyngeal gland cells, only a low amount of fucosylated or paucimannosidic glycans were detected as compared with other insect samples or even bee venom. The unusual modifications of hybrid and multiantennary structures defined here may not only have a physiological role in honeybee development, but represent epitopes recognized by pentraxins with roles in animal innate immunity. © 2018 by The American Society for Biochemistry and Molecular Biology, Inc.

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Denna text är utskriven från följande webbsida:
http://www.gu.se/english/research/publication/?publicationId=274047
Utskriftsdatum: 2019-08-19