Aarhus University Seal / Aarhus Universitets segl

Jens Christian Jensenius

Schistosoma mansoni: adhesion of mannan-binding lectin to surface glycoproteins of cercariae and adult worms

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Schistosoma mansoni is a blood-dwelling trematode which can persist for several years in the vessels of the human host. The schistosomal surface has been extensively characterized by lectin binding studies, revealing the carbohydrate composition of the worm's tegument. Using fluorescent and scanning electron microscopy we demonstrate that the surface carbohydrates of cercariae and adult worms are the binding ligands for mannanbinding lectin (MBL), a serum protein that is part of the innate immune system. An in vitro complement activation assay with C1q-deficient complement suggests that MBL, in association with the serine proteases MASP-1 and MASP-2, is capable of fixing complement components on the schistosomal tegument and activating the complement cascade via the "MBL pathway." MBL is constitutively expressed by hepatocytes and present in the blood at a stable level. Since it is also a weak acute-phase protein and therefore upregulated in an acute-phase response we investigated the serum MBL levels in patients infected with Schistosoma sp. and in healthy control persons. An enzyme-linked immunosorbent assay indicated no differences between the two groups. Although our results suggest an involvement of MBL activated complement in vitro, its role in vivo remains to be clarified.
Original languageEnglish
JournalExperimental Parasitology
Pages (from-to)231-9
Number of pages9
Publication statusPublished - 2000

    Research areas

  • Animals, Carrier Proteins, Collectins, Complement Activation, Female, Humans, Immunoenzyme Techniques, Lectins, Male, Mannans, Membrane Glycoproteins, Mice, Microscopy, Confocal, Microscopy, Electron, Scanning, Microscopy, Fluorescence, Schistosoma mansoni

See relations at Aarhus University Citationformats

ID: 43922073