THE 2012 CHBGS/PROQUEST DISTINGUISHED AWARD WINNER:

B M Nelum K Dorabawila, Ph.D. in Molecular Biotechnology, University of Maryland Eastern Shore, spring 2011

Advisor: Dr. Kwame Nyame

Immunity to Schistosomiasis: Structure, Expression and Immunogenicity of Schistosoma mansoni Glycan Epitope Recognized by the Monoclonal Antibody F2D2

Schistosomiasis is a debilitating disease caused by parasitic helminths of the genus Schistosoma. Glycans are reported to be the most immunogenic molecules of the parasite making them the ideal target molecules for the development of vaccines and serodiagnostics which are urgently needed for disease management. For the identification and purification of immunogenic glycans, we generated a hybridoma that secretes monoclonal antibody (mAb), F2D2, from splenocytes of schsitosome infected mice. Immobilized F2D2 was utilized to affinity purify the schistosome glycan bound by F2D2. Structural characterization by spectroscopic techniques revealed that the purified glycan was the novel fucose containing FLDNF glycan epitope of schistosomes. Analysis of sera from humans and animals infected with schistosomes by glycan microarray of printed purified FLDNF show the epitope is very immnunogenic in humans and animals. We also show by immunohistological staining of intact schistosomes that FLDNF epitopes are abundantly expressed on the surface of the infective larvae and juveniles. Therefore, antibodies raised against FLDNF antigens would be able to bind and effect the elimination of the parasites and thus constitute a potential target antigen for vaccine development. Importantly, we also find that sera from humans infected with other helminthic parasites do not bind the purified FLDNF glycan indicating that the glycans can be used for the specific serodiagnosis of schistosomiasis. Taken together, the results support the use of FLDNF glycans as target antigens for the development of vaccines and serodiagnostics for schistosomiasis.