alexa Components From Inter Alpha Trypsin Inhibitor Protein-glycosaminoglycan-protein Complexes Mediating The Binding To The Domain III From Envelope Protein Of Dengue Virus
ISSN: 2168-958X

Journal of Glycobiology
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3rd Glycobiology World Congress
June 26-28, 2017 London, UK

Dayron Martin Prieto
Center for Genetic Engineering and Biotechnology, Cuba
Posters & Accepted Abstracts: J Glycobiol
DOI: 10.4172/2168-958X-C1-009
Abstract
Dengue disease can be caused by any of the four virus serotypes of dengue virus complex i.e., DV1-4. Symptomatic dengue disease can vary from very mild symptoms to a life threatening syndrome with hemorrhagic manifestations. The interplay between viral and host factors that determine virus pathogenesis is not well understood. In previous work, a proteomic approach was used to study DV interactome in human plasma. Results pointed to inter alpha trypsin inhibitor complexes (IαIc) as putative interaction partners of DV. IαIc consist of protein-glycosaminoglycan-protein structures, containing serum derived Hyaluronan Associated Proteins (SHAP), covalently linked by a chondroitin sulfate chain (CS) with a serine protease inhibitor named Bikunin. SHAP bind covalently to hyaluronic acid in extracellular matrix, enhancing leukocytes adhesion during acute inflammatory response, a process typically altered in patients with severe dengue. Plasma levels of IαIc are lower in children infected with DV and the magnitude of the decrease correlate with disease severity. In this work, IαIc were highly purified from human plasma and identified by mass spectrometry. IαIc components were separated by chemical hydrolysis of CS and used to further validate and characterize the direct interaction with recombinant proteins comprising the domain III of the envelope protein of DV1-4: DIIIE1-4. Two types of independent interactions were identified; one of low affinity with the light chain Bikunin, presumably via the CS chain of this protein and a stronger interaction was found with SHAP. Our results suggest the direct participation of IαIc in the pathogenesis of DV1-4 infection in humans.
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