Haemonchus contortus glycoproteins contain N-linked oligosaccharides with novel highly fucosylated core structures.
Structural studies on the N-linked oligosaccharides of Haemonchus contortus, an economically important nematode that parasitizes domestic ruminants, have revealed core fucosylation of a type not previously observed in any eukaryotic glycoprotein. Mass spectrometric analyses were performed on detergent extracts of homogenized adult H. contortus and on purified H11, a glycoprotein isolated from intestinal brush borders which has been previously shown to be an effective vaccine antigen. The major N-linked glycans identified in the present study have up to three fucose residues attached to their chitobiose cores. The fucoses are found at the 3- and/or 6-positions of the proximal GlcNAc and at the 3-position of the distal GlcNAc. The latter substitution is unique in N-glycans. Most anti-H11 monoclonal antibodies are known to recognize carbohydrate epitopes, and it is possible that the newly discovered multifucosylated core structures are highly immunogenic in this glycoprotein.
Haslam
S M
SM
Department of Biochemistry, Imperial College, London, SW7 2AY, United Kingdom. a.dell@ic.ac.uk
Coles
G C
GC
Munn
E A
EA
Smith
T S
TS
Smith
H F
HF
Morris
H R
HR
Dell
A
A
D000117:Acetylglucosamine / Q000737:chemistry; D000818:Animals; D002240:Carbohydrate Sequence; D005643:Fucose / Q000737:chemistry; D008401:Gas Chromatography-Mass Spectrometry; D006023:Glycoproteins / Q000737:chemistry*; D006189:Haemonchus / Q000737:chemistry*; D015801:Helminth Proteins / Q000737:chemistry*; D008361:Mannosidases / Q000378:metabolism; D008969:Molecular Sequence Data; D012995:Solubility; D044902:beta-Mannosidase
D006023:Glycoproteins; D015801:Helminth Proteins; D005643:Fucose; D008361:Mannosidases; D044902:beta-Mannosidase; D000117:Acetylglucosamine