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J Biol Chem, Vol. 274, Issue 3, 1267-1276, January 15, 1999
§ and
From the Toxoplasma gondii is one of the most
widespread parasites of humans and animals. The parasite has a
remarkable ability to invade a broad range of cells within its
mammalian hosts by mechanisms that are poorly understood at the
molecular level. This broad host cell specificity suggests that
adhesion should involve the recognition of ubiquitous surface-exposed
host molecules or, alternatively, the presence of various parasite
attachment molecules able to recognize different host cell receptors.
We have discovered a sugar-binding activity (lectin) in tachyzoites of
T. gondii that plays a role in vitro in
erythrocyte agglutination and infection of human fibroblasts and
epithelial cells. The ability to agglutinate erythrocytes can be
reversed by a variety of soluble glycoconjugates, of which heparin,
fucoidan, and dextran sulfate were the most effective. Interestingly,
infectivity of tachyzoites for human foreskin fibroblasts, cells that
are commonly used to grow T. gondii in vitro, was increased
by low concentrations of the sulfated glycoconjugates that inhibited
hemagglutination activity (i.e. dextran sulfate and
fucoidan) whereas high concentrations inhibited parasite infection.
Furthermore, inhibition of glycosaminoglycan biosynthesis and sulfation
on the host cells reduced Toxoplasma infectivity. Finally,
Toxoplasma tachyzoites showed a reduced ability to infect
epithelial cell mutants deficient in the biosynthesis of surface
proteoglycans. The probable identity of the hemagglutinin(s) was
investigated by 1) direct binding of red blood cells to filter blots of
Toxoplasma proteins separated by polyacrylamide gel
electrophoresis, and 2) binding of metabolically labeled parasite
proteins to fixed mammalian cells. Three parasite bands were thus
identified as candidate adhesins. These results suggest that attachment
of T. gondii to its target cell is mediated by parasite
lectins and that sulfated sugars on the surface of host cells may
function as a key parasite receptor.
Department of Microbiology & Immunology and
the § Division of Pediatric Infectious Diseases, Lucile
Packard Children's Hospital, Stanford University School of Medicine,
Stanford, California 94305
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