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Göran Larson research group

Glycosylation and disease mechanisms

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Winter vomiting disease and its agent Norovirus (NoV family of Calicivirus), is nowadays recognized as the dominating cause of non bacterial gastroenteritis worldwide. NoV, a small single stranded RNA virus, is an increasing threat to individuals in developing countries (200.000 deaths/year) and in closed settings throughout the world (hospitals, nursing homes, day-care centres, ships etc.). We are studying the carbohydrate binding specificities of NoV virus-like particles to human histo-blood group and secretor gene dependant antigens giving explanations to outbreak variations in individual´s susceptibility to NoV, both at the molecular and at the genetic level. In addition we have identified novel, NoV strain specific, binding specificities to both glycoproteins and to glycosphingolipids and are now, in collaboration with prof. Fredrik Höök, Chalmers, studying the dynamic mechanisms of virus binding to glycosphingolipids in lipid bilayer membranes. By homology modelling and molecular dynamic simulations were are also, together with Per-Georg Nyholm Biognos AB, in the process of screening for and designing appropriate inhibitors of virus adhesion.

Glycosylation is generally recognized as the most complex post translational modification of proteins. A few years ago we started a program to develop new mass spectrometric techniques for characterizing glycoproteins in order to specifically map the glycans while still attached to the amino acid residues of the protein backbone. A first publication came out 2009 in Nature Methods where we introduced a capture and release technology to specifically enrich and characterize sialylated glycoproteins. The technique allowed us to define 36 N-linked and 44 O-linked glycosylation sites on glycoproteins of human cerebrospinal fluid. We have now employed the technique for mapping unique O-glycosylation sites of α-dystroglycan prepared from human skeletal muscle and of glycoproteins of human urine samples. The technology is now being refined for higher sensitivity, better primary and secondary ion fragmentation and applicability to characterize also membrane bound glycoproteins. Structural information on glycosylation and attachment sites of defined glycoproteins are continuously being added to the SwissProt database and thus made publicly searchable through Mascot database searches.

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Group members

Ammi Grahn, PhD
Jonas Nilsson, PhD
Camilla Hesse, PhD,
Inger Johansson, PhD
Gustaf Rydell, PhD
Angelika Kunze, PhD

Adnan Halim, PhD student
Waqas Nasir, PhD student

Sidansvarig: Dan Baeckström|Sidan uppdaterades: 2016-02-26
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