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Antibodies to the Plasmodium falciparum Proteins MSPDBL1 and MSPDBL2 Opsonize Merozoites, Inhibit Parasite Growth, and Predict Protection From Clinical Malaria.

Author information

Affiliations

  • 1. The Walter and Eliza Hall Institute of Medical Research Department of Medical Biology, University of Melbourne, Parkville, Victoria.
      Authors
    • Chiu CY 1
    • Hodder AN 1
    • Lin CS 1
    • Hill DL 1
    • Cowman AF 1
    • Hansen DS 1
    (6 authors)
  • 2. The Walter and Eliza Hall Institute of Medical Research.
      Authors
    • Li Wai Suen CS 2
    (1 author)
  • 3. The Walter and Eliza Hall Institute of Medical Research Australian Institute of Tropical Health and Medicine, James Cook University, Douglas, Queensland, Australia.
      Authors
    • Schofield L 3
    (1 author)
  • 4. Vector Borne Disease Unit, Papua New Guinea Institute of Medical Research, Eastern Highlands Province, Goroka.
      Authors
    • Siba PM 4
    (1 author)
  • 5. The Walter and Eliza Hall Institute of Medical Research Barcelona Center for International Health, University of Barcelona, Spain.
      Authors
    • Mueller I 5
    (1 author)

ORCIDs linked to this article

The Journal of Infectious Diseases, 02 Feb 2015, 212(3):406-415
https://doi.org/10.1093/infdis/jiv057 PMID: 25646353 

Abstract 

Increasing evidence suggests that antibodies against merozoite surface proteins (MSPs) play an important role in clinical immunity to malaria. Two unusual members of the MSP-3 family, merozoite surface protein duffy binding-like (MSPDBL)1 and MSPDBL2, have been shown to be extrinsically associated to MSP-1 on the parasite surface. In addition to a secreted polymorphic antigen associated with merozoite (SPAM) domain characteristic of MSP-3 family members, they also contain Duffy binding-like (DBL) domain and were found to bind to erythrocytes, suggesting that they play a role in parasite invasion. Antibody responses to these proteins were investigated in a treatment-reinfection study conducted in an endemic area of Papua New Guinea to determine their contribution to naturally acquired immunity. Antibodies to the SPAM domains of MSPDBL1 and MSPDBL2 as well as the DBL domain of MSPDBL1 were found to be associated with protection from Plasmodium falciparum clinical episodes. Moreover, affinity-purified anti-MSPDBL1 and MSPDBL2 were found to inhibit in vitro parasite growth and had strong merozoite opsonizing capacity, suggesting that protection targeting these antigens results from ≥2 distinct effector mechanisms. Together these results indicate that MSPDBL1 and MSPDBL2 are important targets of naturally acquired immunity and might constitute potential vaccine candidates.

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Read article at publisher's site: https://doi.org/10.1093/infdis/jiv057

Read article for free, from open access legal sources, via Unpaywall: https://academic.oup.com/jid/article-pdf/212/3/406/13806113/jiv057.pdfUnpaywall

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