ArticleThe Journal of biological chemistry2009
Structural characterization of the bradyzoite surface antigen (BSR4) from Toxoplasma gondii, a unique addition to the surface antigen glycoprotein 1-related superfamily.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Molecular characterization ofRoyal Society open science · 2025Article
- The determinants regulatingFrontiers in microbiology · 2022Review
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- Structure of the Pf12 and Pf41 heterodimeric complex ofFEMS microbes · 2022Article
- The structure of a major surface antigen SAG19 from Eimeria tenella unifies the Eimeria SAG family.Communications biology · 2021Article
- Nanobody generation and structural characterization of Plasmodium falciparum 6-cysteine protein Pf12p.The Biochemical journal · 2021Article
- Congenital Transmission of Apicomplexan Parasites: A Review.Frontiers in microbiology · 2021Review
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- Multimeric assembly of host-pathogen adhesion complexes involved in apicomplexan invasion.PLoS pathogens · 2014Article
- Crystallization and preliminary crystallographic analysis of a surface antigen glycoprotein, SAG19, from Eimeria tenella.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- SAG2A protein from Toxoplasma gondii interacts with both innate and adaptive immune compartments of infected hosts.Parasites & vectors · 2013Article
- Structural and biochemical characterization of Plasmodium falciparum 12 (Pf12) reveals a unique interdomain organization and the potential for an antiparallel arrangement with Pf41.The Journal of biological chemistry · 2013Article
- Analysis of structures and epitopes of surface antigen glycoproteins expressed in bradyzoites of Toxoplasma gondii.BioMed research international · 2013Article
- Structure of the Plasmodium 6-cysteine s48/45 domain.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Biochemical and functional analysis of two Plasmodium falciparum blood-stage 6-cys proteins: P12 and P41.PloS one · 2012Article
- Structural and functional characterization of SporoSAG: a SAG2-related surface antigen from Toxoplasma gondii.The Journal of biological chemistry · 2010Article
- Observations on bradyzoite biology.Microbes and infectionReview
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Authors and funding
6 authors at 3 institutions in 3 countries.
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Abstract
Toxoplasma gondii is an obligate intracellular protozoan parasite that infects nearly one-third of the human population. The success of T. gondii is based on its complex life cycle; a lytic tachyzoite form disseminates infection, whereas an encysted bradyzoite form establishes a latent, chronic infection. Persistence and transmissibility is central to the survival of the parasite and is, in part, mediated by a family of antigenically distinct surface antigen glycoprotein (SAG)-related sequences (SRS) adhesins that play a dual role in host cell attachment and host immune evasion. More than 160 members of the SRS family have been identified with only the tachyzoite-expressed SAG1 structurally characterized. Here we report the first structural description of the bradyzoite adhesin BSR4 using x-ray crystallography and small angle x-ray scattering. The 1.90-A crystal structure of BSR4 reveals an architecture comprised of tandem beta sandwich domains organized in a head to tail fashion with the N-terminal domain responsible for dimer formation. A restructured topology in BSR4 results in a ligand-binding site that is significantly reorganized in both structure and chemistry relative to SAG1, consistent with BSR4 binding a distinct physiological ligand. The small angle x-ray scattering solution structure of BSR4 highlights a potentially important structural role for the interdomain polymorphic linker that imparts significant flexibility that may promote structural adaptation during ligand binding. This study reveals an unexpected level of structural diversity within the SRS superfamily and provides important insight into the role of these virulence factors.
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