The "sweeter" side of what we do

The "sweeter" side of what we do

On the fringe of biochemistry is a small but friendly group of scientists with one thing in common-- a proclivity for sugars or carbohydrates or as we call it "glycans".
DEFINITIONS

Required reading:
Essentials of Glycobiology. Edited by Ajit Varki, Richard Cummings, Jeffrey Esko, Hudson Freeze, Gerald Hart, and Jamey Marth.  Cold Spring Harbor (NY): CSHL Press. 1999.
Drickamer, K; M.E. Taylor (2006). Introduction to Glycobiology  (2nd ed.). Oxford University Press, USA.

RESEARCH QUESTIONS
Glycosylation affects both cell-cell contact and communication as well as critical intracellular processes involved in cell development.  As such, in the context of malaria transmission biology, my lab is focused on tackling through a multi-OMICs strategy the following key research questions:

  • What are the glycan, glycolipid and glycoprotein ligands on the mosquito midgut apical microvillar surface that act as ligands for Plasmodium ookinete attachment and invasion?
  • What are the glycan, glycolipid and glycoprotein ligands on the basal side of the mosquito salivary glands that act as ligands for Plasmodium sporozoite attachment and invasion?
  • How is parasite attachment and invasion of midgut or salivary glands affected by the absence of the glycan modification although the polypeptide backbone is retained?
  • What is the spectrum of diversity of glycan modifications in the midgut and salivary glands and how does such diversity impact vector host-parasite interactions?
  • Plasmodium ookinete and sporozoite surface proteins appear to be devoid of any glycosylation modification except for the parasite-specific glycosylphosphotidylinositol anchor, suggesting a highly conserved and critical strategy for displaying proteins on the plasmalemma.  Can we target the enzymes involved in GPI anchor through rational drug design to disrupt parasite development?
  • Cytosolic O-linked GlcNacylation is highly conserved across eukaryotes, yet remains controversial for Plasmodium?  O-GlcNAc modifications have been shown to influence a variety of important cellular processes necessary for survival, development and defense.  Does Plasmodium have the necessary machinery for O-GlcNAcylation?  Do such modifications exist in nature and if so, what proteins are O-GlcNAcylated in Plasmodium during the course of its development?

DINGLASAN LABORATORY

EMERGING PATHOGENS INSTITUTE

THE UNIVERSITY OF FLORIDA

Department of Infectious Diseases & Pathology
COLLEGE OF VETERINARY MEDICINE
2055 Mowry Road, Rm 375
Tel. +1 (352) 294-8448 (OFFICE) / Tel. +1 (410) 294-8470 (LAB Rm. 320-326)

 

 

 

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