Major O-glycans in the spores of two microsporidian parasites are represented by unbranched manno-oligosaccharides containing α-1,2 linkages
Protein glycosylation in microsporidia, a fungi-related group comprising exclusively obligate intracellular parasitic species, is still poorly documented. Here, we have studied glycoconjugate localization and glycan structures in spores of Encephalitozoon cuniculi and Antonospora locustae, two dista...
Saved in:
Published in | Glycobiology (Oxford) Vol. 17; no. 1; pp. 56 - 67 |
---|---|
Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Oxford University Press
2007
Oxford University Press (OUP) |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Protein glycosylation in microsporidia, a fungi-related group comprising exclusively obligate intracellular parasitic species, is still poorly documented. Here, we have studied glycoconjugate localization and glycan structures in spores of Encephalitozoon cuniculi and Antonospora locustae, two distantly related microsporidians invading mammalian and insect hosts, respectively. The polar sac-anchoring disc complex or polar cap, an apical element of the sporal invasion apparatus, was strongly periodic acid-thiocarbohydrazide-Ag proteinate-positive. Mannose-binding lectins reacted with the polar cap and recognized several bands (from 20 to 160 kDa) on blots of E. cuniculi protein extracts. Physicochemical analyses provided the first determination of major glycostructures in microsporidia. O-linked glycans were demonstrated to be linear manno-oligosaccharides containing up to eight α1, 2-linked mannose residues, thus resembling those reported in some fungi such as Candida albicans. No N-linked glycans were detected. The data are in accordance with gene-based prediction of a minimal O-mannosylation pathway. Further identification of individual mannoproteins should help in the understanding of spore germination mechanism and host-microsporidia interactions. |
---|---|
Bibliography: | istex:FDFD3722C3B42BA763B2BF02BD1D9D2B8CD525E1 ArticleID:cwl050 ark:/67375/HXZ-CXP8K9VB-F ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0959-6658 1460-2423 |
DOI: | 10.1093/glycob/cwl050 |