Mj. Mcconville, THE SURFACE GLYCOCONJUGATES OF PARASITIC PROTOZOA - POTENTIAL TARGETSFOR NEW DRUGS, Australian and New Zealand Journal of Medicine, 25(6), 1995, pp. 768-776
Protozoan parasites are the cause of many diseases in humans and their
domestic livestock. Glycoconjugates (i.e. glycoproteins, glycolipids)
on the cell surface of these extremely diverse and very primative euk
aryotes play a crucial rot in determining the specificity of the host-
parasite interaction and in protecting the parasites within their resp
ective hosts. These molecules frequently share a common structural fea
ture in that they are attached to the plasma membrane via a glycosylph
osphatidylinositol (GPI) glycolipid. While GPI protein-membrane anchor
s are ubiquitous among the eukaryotes, riley are used with exceptional
ly high frequency in the protozoa. Some kinetopastid parasites also sy
nthesise very high levels of GPI-related glycolipids that are not link
ed to protein. Thus GPI-anchored molecules or free GPI glycolipids ten
d to dominate the cell surface molecular architecture of these organis
ms. The highly elevated levels and specialised nature of GPI metabolis
m in rhp Kinetoplastid and other parasites suggests that the GPI biosy
nthetic pathway might be a good target for the development of new chem
otherapeutic agents. This article reviews the wide range of functions
that GPI protein anchors and GPI-related glycolipids are thought to pe
rform in these organisms and some aspects of their biosynthesis.