ABSTRACT
Cell surface of leishmaniasis causal agent, a parasitic member of Protozoa of Leishmania genus, is covered by thick glycocalix consisting of various phosphatidylinositol-anchored molecules. This review deals with the structure and biosynthesis of the main phosphoglycans and glycoproteins of Leishmania cell surface, many of which incorporate the rare natural D-arabinopyranose, and the problem concerning the involvement of these molecules in support of Leishmania survival during their intricate life cycle is discussed.
Subject(s)
Glycoconjugates/chemistry , Leishmania/metabolism , Arabinose/chemistry , Glycoconjugates/biosynthesis , Glycoconjugates/physiology , Glycolipids/chemistry , Glycolipids/metabolism , Glycosphingolipids/biosynthesis , Glycosphingolipids/chemistry , Membrane Proteins/biosynthesis , Membrane Proteins/chemistry , Metalloendopeptidases/chemistry , Metalloendopeptidases/metabolism , Proteoglycans/biosynthesis , Proteoglycans/chemistry , Protozoan Proteins/biosynthesis , Protozoan Proteins/chemistryABSTRACT
In this work we describe an unusual enzyme from Leishmania major (Arabinokinase/Pyrophosphorylase) that catalyzes the synthesis of GDP-D-arabinopyranose (GDP-D-Arap) via a D-arabinose-1-phosphate intermediate in the presence of ATP and GTP. Our data indicate GDP-D-Arap transport in vivo by the LPG2 multispecific nucleotide sugar transporter into the Leishmania Golgi apparatus, in which it can be used by glycosyltransferases as a donor substrate for glycosylation.
