Journal of Glycobiology
Open Access

Design and development of glycopeptides as multiple sclerosis diagnostic probe

Glycobiology World Congress

August 10-12, 2015 Philadelphia, USA

Anna Maria D�¢����Ursi

Posters-Accepted Abstracts: J Glycobiol

Abstract :

Post translational modifications such as glycosylation may play a fundamental role for specific auto antibody recognition. In
particular glycoproteins may be recognized as not-self molecules by antibodies triggering the onset of severe autoimmune
diseases. We have previously demonstrated that an aberrant N-glucosylation is a fundamental determinant of auto-Ab
recognition in multiple sclerosis (MS). The N-glucosylated Asn present in the 30-50 fragment of the myelin oligodentrocyte
glycoprotein (MOG (30-50)) is an immunogenic epitope responsible for the interaction with MS auto antibodies. Starting from
this sequence we identified CSF114 (Glc) biomarker, a glycopeptides able to recognize by ELISA, specific IgM auto Abs in the
sera of MS patient population. CSF114 was improved in its specificity and sensitivity leading to the optimized glycopeptides
SP077. This showed a higher homology with CSF114 (Glc) but was able to detect higher antibody titers as compared to CSF114
(Glc). NMR and ESR experiments supported by computer simulations allowed characterizing the sequence of events that rule
the antigenic activity of the mentioned immunogenic peptides. These studies show that the glycosidic moiety plays a pivotal
role, first ruling the binding of the probe to the membrane and then in coordinating the interaction with the antibody. Our
findings provide valuable hints to develop new effective MS glycosylated probes and propose an innovative methodological
approach that is instrumental to investigate the functional mechanism of other biologically relevant glycopeptides.