z-logo
Premium
Atomic resolution insight into host cell recognition by Toxoplasma gondii
Author(s) -
Blumenschein Tharin MA,
Friedrich Nikolas,
Childs Robert A,
Saouros Savvas,
Carpenter Elisabeth P,
CampaneroRhodes Maria A,
Simpson Peter,
Chai Wengang,
Koutroukides Theodoros,
Blackman Michael J,
Feizi Ten,
SoldatiFavre Dominique,
Matthews Stephen
Publication year - 2007
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7601704
Subject(s) - biology , toxoplasma gondii , host (biology) , toxoplasmosis , computational biology , virology , genetics , antibody
The obligate intracellular parasite Toxoplasma gondii , a member of the phylum Apicomplexa that includes Plasmodium spp., is one of the most widespread parasites and the causative agent of toxoplasmosis. Micronemal proteins (MICs) are released onto the parasite surface just before invasion of host cells and play important roles in host cell recognition, attachment and penetration. Here, we report the atomic structure for a key MIC, TgMIC1, and reveal a novel cell‐binding motif called the microneme adhesive repeat (MAR). Using glycoarray analyses, we identified a novel interaction with sialylated oligosaccharides that resolves several prevailing misconceptions concerning TgMIC1. Structural studies of various complexes between TgMIC1 and sialylated oligosaccharides provide high‐resolution insights into the recognition of sialylated oligosaccharides by a parasite surface protein. We observe that MAR domains exist in tandem repeats, which provide a highly specialized structure for glycan discrimination. Our work uncovers new features of parasite–receptor interactions at the early stages of host cell invasion, which will assist the design of new therapeutic strategies.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here