Structure of the immunodominant surface antigen from the toxoplasma gondii SRS superfamily

Xiao lin He, Michael E. Grigg, John C. Boothroyd, K. Christopher Garcia

Research output: Contribution to journalArticlepeer-review

89 Scopus citations

Abstract

Toxoplasma gondii is a persistent protozoan parasite capable of infecting almost any warm-blooded vertebrate. The surface of Toxoplasma is coated with a family of developmentally regulated glycosylphosphatidylinositol (GPI)-linked proteins (SRSs), of which SAG1 is the prototypic member. SRS proteins mediate attachment to host cells and interface with the host immune response to regulate the virulence of the parasite. The 1.7 Å structure of the immunodominant SAG1 antigen reveals a homodimeric configuration in which the dimeric interface is mediated by an extended β-sheet that forms a deep groove lined with positively charged amino acids. This basic groove seems to be conserved among SRS proteins and potentially serves as a sulfated proteoglycan-binding site on target cell surfaces, thus rationalizing the promiscuous attachment properties of Toxoplasma to a broad range of host cell types.

Original languageEnglish (US)
Pages (from-to)606-611
Number of pages6
JournalNature Structural Biology
Volume9
Issue number8
DOIs
StatePublished - 2002

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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