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The essential mosquito-stage P25 and P28 proteins from Plasmodium form tile-like triangular prisms

Nature Structural & Molecular Biology volume 13, pages 9091 (2006) | Download Citation

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Abstract

P25 and P28 proteins are essential for Plasmodium parasites to infect mosquitoes and are leading candidates for a transmission-blocking malaria vaccine. The Plasmodium vivax P25 is a triangular prism that could tile the parasite surface. The residues forming the triangle are conserved in P25 and P28 from all Plasmodium species. A cocrystal structure shows that a transmission-blocking antibody uses only its heavy chain to bind Pvs25 at a vertex of the triangle.

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Acknowledgements

We thank the Malaria Vaccine Development Branch of the NIAID for Pvs25 and Y.T. Bryceson of NIAID for cDNA synthesis. X-ray data were collected at the SER-CAT 22-ID and SBC-CAT 19-ID beamlines at the Advanced Photon Source, which are supported by the US Department of Energy, Office of Science, Office of Basic Energy Sciences under contract W-31-109-Eng-38. This research was supported by the intramural research programs of the NIH and NIAID.

Author information

Author notes

    • Ajay K Saxena
    •  & Anthony W Stowers

    Present addresses: School of Life Sciences, Room-403, Jawaharlal Nehru University, New Mehrauli Road, New Delhi, 110067, India (A.K.S.) and CSL Limited ACN 051 588 348, 45 Poplar Road, Parkville, Victoria 3052, Australia (A.W.S.).

Affiliations

  1. Structural Biology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases (NIAID), US National Institutes of Health (NIH), Twinbrook 2, 12441 Parklawn Drive, Rockville, Maryland 20852, USA.

    • Ajay K Saxena
    • , Kavita Singh
    • , Hua-Poo Su
    • , Michael M Klein
    •  & David N Garboczi
  2. Malaria Vaccine Development Branch, NIAID, NIH, Twinbrook 1, 5640 Fishers Lane, Rockville, Maryland, 20852, USA.

    • Anthony W Stowers
    • , Allan J Saul
    •  & Carole A Long

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Competing interests

The authors declare no competing financial interests.

Corresponding authors

Correspondence to Ajay K Saxena or David N Garboczi.

Supplementary information

PDF files

  1. 1.

    Supplementary Fig. 1

    Pvs25 EGF-like domains and their interactions.

  2. 2.

    Supplementary Fig. 2

    Sequence alignment of Pvs25 and other P25 molecules.

  3. 3.

    Supplementary Fig. 3

    Sequence alignment of Pvs25 and P28 molecules.

  4. 4.

    Supplementary Fig. 4

    Electron density at the Pvs25-Fab interface.

  5. 5.

    Supplementary Table 1

    Data collection and refinement statistics.

  6. 6.

    Supplementary Table 2

    Hydrogen bonds between domain 1 and domains 3 and 4 of Pvs25.

  7. 7.

    Supplementary Table 3

    Contacting residues between Pvs25 and the 2A8 Fab VH domain.

  8. 8.

    Supplementary Methods

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DOI

https://doi.org/10.1038/nsmb1024

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