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© Valérie Choumet
Mosquitoes were orally infected with the chikungunya virus. Midguts were dissected at day 5 post-infection, fixed and permeabilised. Virus is shown in red (anti-E2 protein, cyanine 3), the actin network in green (phalloidin 548) and nuclei in blue (DAPI).
Publication : Journal of natural medicines

A Tn antigen binding lectin from Myrsine coriacea displays toxicity in human cancer cell lines

Team: Archived: Protein conjugates
Member: Sylvie Bay
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of natural medicines - 30 May 2012

Medeiros A, Berois N, Incerti M, Bay S, Franco Fraguas L, Osinaga E

Link to Pubmed [PMID] – 22645079

J Nat Med 2013 Apr;67(2):247-54

The Tn antigen (GalNAc-O-Ser/Thr) is one of the most specific human cancer-associated structures. In the present study we characterize the biochemical and functional properties of the Myrsine coriacea lectin (McL). We show that McL is an unusual high molecular weight highly glycosylated protein, which displays a strong Tn binding activity. The lectin exhibits in vitro inhibition of proliferation in the six cancer cell lines evaluated, in a dose-dependent manner (the strongest activity being against HT-29 and HeLa cells), whereas it does not exhibit toxicity against normal lymphocytes. McL could be exploited in the design of potential new tools for the diagnosis or treatment of cancer.