Emma Del Real


Education: Bachelor of Science in biology (December 2014)

McNair Project: Role of Post-translational Modifications of a Viral Fibroblast Growth Factor on Virulence (2009)

Mentor: Lorena Passerelli, Ph.D.

Baculoviruses are enveloped viruses, containing a large, circular and double-stranded DNA genome. Most baculovirus encode a viral fibroblast growth factor (vfgf) that is homologous to the fibroblast growth factors (fgfs) found in both invertebrate and vertebrate organisms. FGFs have a wide range of functions that include working as mitogens and motogens and are involved in processes such as neural cell differentiation, osteogenesis, angiogenesis, and limb formation. The vfgf of the Bombyx morinucleopolyhedrovirus (BmNPV) is N-glycosylated and readily secreted. On the other hand, the vfgf of the Autographa californica MNPV (AcMNPV) is not N-glycosylated. We are constructing recombinant viruses where N-glycosylation sites are altered or introduced in the BmNPV and the AcMNPV fgfs, respectively. This will allow us to determine the role of N-glycosylation during virus infection both in in vitro cell culture systems and in vivo.

McNair Project: Effects of a Viral Fibroblast Growth Factor N-Glycosylation Modifications on Virulence (2010)

Mentor: Lorena Passarelli, Ph.D.

Baculoviruses are rod-shaped enveloped viruses with circular, double-stranded DNA genomes. Most baculoviruses carry a fibroblast growth factor (vfgf) that is homologous to fgfs. FGFs exhibit a broad range of functions during cellular development. FGFs may be posttranslationally modified by addition of sugar chains (N-gylcans) that may affect folding, secretion, and activity. The vFGF of Bombyx mori nucleopolyhedrovirus (BmNPV) is N-glyocsylated, secreted and affects virus replication in cell culture and its host. In contrast, the vFGF of Autographa californica mNPV (AcMNPV) is not N-glycosylated - yet secreted - and its activity is important only during in vivo infections. In this study, we constructed recombinant viruses where sites for N-gylcosylation were altered or introduced in the BmNPV and AcMNPV fgfs, respectively. We hypothesize that N-gylosylation of AcMNPV FGF enhances secretion and results in more robust effects both in vitro and in vivo. Similarly, eliminating N-glycosylation from the BmNPV FGF would result in a phenotype similar to the AcMNPV FGF. We are currently characterizing the altered vFGFs by determining N-glycosylation patterns, effects on virus replication and virulence. This will allow us to determine the role of vFGF N-glycosylation during virus replication, a potential tool for the development of improved biological insecticides.