Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Structures of monomeric and oligomeric forms of the Toxoplasma gondiiperforin-like protein 1

Tools
- Tools
+ Tools

Ni, Tao, Williams, Sophie I., Rezelj, Saša, Anderluh, Gregor, Harlos, Karl, Stansfeld, Phillip J. and Gilbert, Robert J. C. (2018) Structures of monomeric and oligomeric forms of the Toxoplasma gondiiperforin-like protein 1. Science Advances, 4 (3). eaaq0762. doi:10.1126/sciadv.aaq0762

[img]
Preview
PDF
WRAP-structures-monomeric-oligomeric-perforin-protein-Stansfeld-2018.pdf - Published Version - Requires a PDF viewer.
Available under License Creative Commons Attribution 4.0.

Download (1106Kb) | Preview
Official URL: http://dx.doi.org/10.1126/sciadv.aaq0762

Request Changes to record.

Abstract

Toxoplasma and Plasmodium are the parasitic agents of toxoplasmosis and malaria, respectively, and use perforin-like proteins (PLPs) to invade host organisms and complete their life cycles. The Toxoplasma gondii PLP1 (TgPLP1) is required for efficient exit from parasitophorous vacuoles in which proliferation occurs. We report structures of the membrane attack complex/perforin (MACPF) and Apicomplexan PLP C-terminal β-pleated sheet (APCβ) domains of TgPLP1. The MACPF domain forms hexameric assemblies, with ring and helix geometries, and the APCβ domain has a novel β-prism fold joined to the MACPF domain by a short linker. Molecular dynamics simulations suggest that the helical MACPF oligomer preserves a biologically important interface, whereas the APCβ domain binds preferentially through a hydrophobic loop to membrane phosphatidylethanolamine, enhanced by the additional presence of inositol phosphate lipids. This mode of membrane binding is supported by site-directed mutagenesis data from a liposome-based assay. Together, these structural and biophysical findings provide insights into the molecular mechanism of membrane targeting by TgPLP1.

Item Type: Journal Article
Subjects: Q Science > QL Zoology
Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Toxoplasma gondii, Plasmodium, Proteins
Journal or Publication Title: Science Advances
Publisher: American Association for the Advancement of Science
ISSN: 2375-2548
Official Date: 2 March 2018
Dates:
DateEvent
2 March 2018Published
Volume: 4
Number: 3
Article Number: eaaq0762
DOI: 10.1126/sciadv.aaq0762
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
MR/N000331/1Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
BB/M011224/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
090532/Z/09/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
060208/Z/00/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
BB/I019855/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/P01948X/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/R002517/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
UNSPECIFIEDWellcome Trusthttp://dx.doi.org/10.13039/100010269
P1-0391Javna Agencija za Raziskovalno Dejavnost RShttp://dx.doi.org/10.13039/501100004329

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics

twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us