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J. Biol. Chem., Vol. 277, Issue 51, 49143-49157, December 20, 2002
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From the We report the fine structure of a nearly
contiguous series of N-glycans from the soil nematode
Caenorhabditis elegans. Five major classes are revealed
including high mannose, mammalian-type complex, hybrid,
fuco-pausimannosidic (five mannose residues or fewer substituted with
fucose), and phosphocholine oligosaccharides. The high mannose,
complex, and hybrid N-glycan series show a high degree of
conservation with the mammalian biosynthetic pathways. The
fuco-pausimannosidic glycans contain a novel terminal fucose substitution of mannose. The phosphocholine oligosaccharides are high
mannose type and are multiply substituted with phosphocholine. Although
phosphocholine oligosaccharides are known immunomodulators in human
nematode and trematode infections, C. elegans is unique as
a non-parasitic nematode containing phosphocholine
N-glycans. Therefore, studies in C. elegans
should aid in the elucidation of the biosynthetic pathway(s) of this
class of biomedically relevant compounds. Results presented here show
that C. elegans has a functional orthologue for nearly
every known enzyme found to be deficient in congenital disorders of
glycosylation types I and II. This nematode is well characterized
genetically and developmentally. Therefore, elucidation of its
N-glycome, as shown in this report, may place it among the
useful systems used to investigate human disorders of glycoconjugate
synthesis such as the congenital disorders of glycosylation syndromes.
The Fine Structure of Caenorhabditis elegans
N-Glycans*,
,¶
Department of Molecular and Cell Biology,
Boston University, Goldman School of Dental Medicine and
§ Mass Spectrometry Resource, Department of Biochemistry,
Boston University School of Medicine,
Boston, Massachusetts 02118-2526
*
This work was supported by National Institute of Health
Grant GM 30365 (to C. H.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains Figs. 1 and 2.
¶
To whom correspondence should be addressed: Dept. of Molecular
and Cell Biology, Boston University Goldman School of Dental Medicine,
715 Albany St., Evans 437, Boston, MA 02118. Tel.: 617-414-1040; Fax:
617-414-1041; E-mail: chirschb@bu.edu.
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