Variation in the nature of attachment of phosphorylcholine to excretory-secretory products of adult Brugia pahangi

The mechanism of linkage of phosphorylcholine (PC) to excretory-secretory products (ES) of adult Brugia pahangi has been investigated. Biosynthetic radio-isotope labelling of ES with [3H]choline followed by SDS-PAGE/fluorography revealed a smear of molecular weight approximately 40-100 kDa which los...

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Bibliographic Details
Published inParasitology Vol. 114 ( Pt 3); p. 257
Main Authors Nor, Z M, Houston, K M, Devaney, E, Harnett, W
Format Journal Article
LanguageEnglish
Published England 01.03.1997
Subjects
Amidohydrolases - metabolism
Animals
Antigens, Helminth - chemistry
Antigens, Helminth - metabolism
Blotting, Western
Brugia pahangi - chemistry
Brugia pahangi - immunology
Electrophoresis, Polyacrylamide Gel
Helminth Proteins - chemistry
Helminth Proteins - metabolism
Molecular Weight
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Phosphorylcholine - chemistry
Phosphorylcholine - metabolism
Polysaccharides - chemistry
Polysaccharides - metabolism
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Summary:The mechanism of linkage of phosphorylcholine (PC) to excretory-secretory products (ES) of adult Brugia pahangi has been investigated. Biosynthetic radio-isotope labelling of ES with [3H]choline followed by SDS-PAGE/fluorography revealed a smear of molecular weight approximately 40-100 kDa which loses its radiolabel following exposure to N-glycosidase F, but not mild alkali. PC is thus attached to this smear of molecules via N-type glycans, a mechanism of linkage previously observed with respect to PC-ES of Acanthocheilonema viteae. Western blotting analysis of non-radiolabelled ES demonstrated the existence of additional PC-ES which were insensitive to N-glycosidase F, but not to alkali. This second group of molecules is therefore likely to contain PC linked to O-glycans. Filarial nematodes may thus utilize 2 classes of glycan for attachment of PC. Examination of B. pahangi and A. viteae whole worm extracts by Western blotting indicated that their PC content could not be cleaved by N-glycosidase F and hence the use of N-type glycans may be restricted to a subset of ES products. The implications of these findings with respect to developing inhibitors of PC attachment for use as anti-filarial drugs are discussed.
ISSN:0031-1820
DOI:10.1017/S0031182096008402