Discipline: Biological Sciences
Subcategory: Biochemistry (not Cell and Molecular Biology and Genetics)
Keilon Robinson - Texas Southern University
Co-Author(s): Jorge Rodriguez, Bernadette Ezeabikwa, Msano Mandalasi, and Kwame Nyame, University of Maryland Eastern Shore, Princess Anne, MD
Schistosomes are parasitic blood flukes that cause schistosomiasis, a vascular disease that affects 240 million people worldwide. There are three main species that infect humans namely; Schistosoma mansoni, Schistosoma japonicum and Schistosoma haematobium. Diagnosis of infections are done by microscopic examination of stool and urine samples from infected hosts while treatment relies on a single chemotherapeutic agent. Vaccines and serodiagnostics are needed to augment and improve the current treatment and diagnostic options. Studies have shown that the major antibody responses in individuals infected with schistosomes are directed against glycans or carbohydrate antigens synthesized by the parasites making these glycans potential targets for both vaccines and serodiagnosis. The structures of the immunogenic glycans have now been found to be lacdiNAc (LDN; GalNAcĪ²14GlcNAc) glycan epitopes and their fucosylated derivatives present on N-glycans. Interestingly, bovine milk glycoproteins also have N-glycan structures with LDN outer branches very much like the structures of schistosome glycan antigens and thus constitute potentially cheap source of LDN bearing Nglycans that can be remodeled to schistosome-type antigenic glycans for evaluation as vaccine and serodiagnostic targets. We have evaluated nonfat dry milk and heifer colostrum for the levels of expression of LDN bearing N-glycans and find that glycoproteins from heifer colostrum express higher levels of LDN epitope. Further, heifer colostrum lacks casein, a nonglycosylated protein abundantly found in nonfat dry milk. Thus, heifer colostrum is a better milk product for preparation of LDN bearing N-glycans. We have prepared lactose free, delipidated, dried colostrum for release of the N-glycans from the glycoproteins.
Funder Acknowledgement(s): Funding provided by National Science Foundation (NSF) Living Marine Resources Cooperative Science Center (LMRCSC).
Faculty Advisor: Bobby Wilson,