Fasciola hepatica (Fh), commonly known as liver fluke, is a trematode helminth which causes fasciolosis in ruminants and humans. The outer component of the parasite, the tegument, is the sole biological matrix that remains continually exposed to the host immune system. Many of the tegumental proteins carry glycans as post-translational modification.
Glycans and glycoconjugates play a crucial role in the biology of helminth infections by driving the host immune response towards Th2 type [1]. The majority of studies on immune modulatory helminth glycans to date have focused on the Schistosoma mansoni derived Lacto-N-fucopentaose III (LNFP III) and Lewisxconjugates [2].
To date no systematic study has been carried out to accurately profile the glycans decorating Fh tegumental proteins. This work represents a preliminary approach to study Fh tegument-derived N-and O-linked glycans. In this study, the presence of glycoconjugates was initially investigated by the means of lectin blots and histology. A full characterization of such glycans was then performed by the use of mass spectrometric techniques. To the best of the authors knowledge this is the first ever glycoanalytical study of Fasciola hepatica tegument-derived glycoproteins.
1. van Die I, Cummings RD (2010) Glycan gimmickry by parasitic helmints: a strategy for modulating the host immune response? Glycobiology 20:2-12
2. Hokke CH, Deelder AM, Hoffmann KF, Whurer M. (2007) Glycomics-driven discoveries in schistosome research. Exp Parasitol. 117:275-83
