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PreprintCited by 15Toxoplasma gondii Research StudiesMalaria Research and ControlCoccidia and coccidiosis research

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Structural and regulatory insights into the glideosome-associated connector from Toxoplasma gondii

Open access
Kumar, Amit, Vadas, Oscar, Dos Santos Pacheco, Nicolas, Zhang, Xu, Chao, Kin, Darvill, Nicolas, Rasmussen, Helena Ø., Xu, Yingqi, Lin, Gloria, Stylianou, Fisentzos A, Pedersen, Jan Skov, Rouse, Sarah L., Morgan, Marc L., Soldati-Favre, Dominique, Matthews, Steve·2023·eLife
DOI 10.1101/2023.01.23.525158PMC PMC10125020

Preprint — published as 10.7554/elife.86049 · Paper page

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Abstract

The phylum of Apicomplexa groups intracellular parasites that employ substratedependent gliding motility to invade host cells, egress from the infected cells and cross biological barriers. The glideosome associated connector (GAC) is a conserved protein essential to this process. GAC facilitates the association of actin filaments with surface transmembrane adhesins and the efficient transmission of the force generated by myosin translocation of actin to the cell surface substrate. Here, we present the crystal structure of Toxoplasma gondii GAC and reveal a unique, supercoiled armadillo repeat region that adopts a closed ring conformation. Characterisation of the membrane binding interface within the C-terminal PH domain as well as an N-terminal fragment necessary for association with F-actin suggest that GAC adopts multiple conformations. A multi-conformational model for assembly of GAC within the glideosome is proposed.

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Metadata

Authors
Kumar, A., Vadas, O., Dos Santos Pacheco, N., Zhang, X., Chao, K., Darvill, N., Rasmussen, H. Ø., Xu, Y., Lin, G., Stylianou, F. A., Pedersen, J. S., Rouse, S. L., Morgan, M. L., Soldati-Favre, D., & Matthews, S.
Affiliations
  • Imperial College London (GB)
  • University of Geneva (CH)
  • Aarhus University (DK)
ORCID
Venue
eLife
Publisher
openRxiv
Published
2023-01-23
Volume
12
ISSN
2050-084X (ISSN-L)
DOI
10.1101/2023.01.23.525158
PMC
PMC10125020
OpenAlex
W4362520906
Cited by
15
References
1
Citations by year
2026: 5 · 2025: 3 · 2024: 4 · 2023: 3
FWCI
3.52
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • eLife (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Spiral (Imperial College London) (submittedVersion, cc-by)
  • Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
Funders
  • National Science Foundation
  • Wellcome Trust (202926/Z/16/Z)
  • Diamond Light Source
  • Leverhulme Trust (RPG-2018-107)
  • Imperial College London (BB/W001764/1, RPG_2018_107)
  • Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (185325, 198545)
  • Danmarks Frie Forskningsfond (8021-00133B)
  • Université de Genève
  • Directorate for Biological Sciences
  • Swiss Re Foundation (CRSII5_198545, 10030_185325)
  • Biotechnology and Biological Sciences Research Council (BB/D524840/1, 202926/Z/16/Z, BB/W001764/1)
Topics
  • Life Sciences › Immunology and Microbiology › Parasitology › Toxoplasma gondii Research Studies
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Malaria Research and Control
  • Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Coccidia and coccidiosis research
Keywords
Toxoplasma gondii, gliding motility, armadillo repeats, protein crystal structure, actin binding, membrane binding, Apicomplexa
MeSH terms
Actins, Cell Membrane, Actin Cytoskeleton, Myosins, Toxoplasma, Protozoan Proteins

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