Plasmodium falciparum merozoite surface protein 1 blocks the proinflammatory protein S100P

Michael Waisberg, Gustavo C. Cerqueira, Stephanie B. Yager, Ivo M.B. Francischetti, Jinghua Lu, Nidhi Gera, Prakash Srinivasan, Kazutoyo Miura, Balazs Rada, Jan Lukszo, Kent D. Barbian, Thomas L. Leto, Stephen F. Porcella, David L. Narum, Najib El-Sayed, Louis H. Miller, Susan K. Pierce

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Themalaria parasite, Plasmodiumfalciparum, and the human immune system have coevolved to ensure that the parasite is not eliminated and reinfection is not resisted. This relationship is likely mediated through a myriad of host-parasite interactions, although surprisingly few such interactions have been identified.Herewe showthat the 33-kDa fragment of P. falciparum merozoite surface protein 1 (MSP1 33), an abundant protein that is shed during red blood cell invasion, binds to the proinflammatory protein, S100P. MSP1 33 blocks S100P-induced NFκB activation inmonocytes and chemotaxis in neutrophils. Remarkably, S100P binds to both dimorphic alleles of MSP1, estimated to have diverged >27 Mya, suggesting an ancient, conserved relationship between these parasite and host proteins that may serve to attenuate potentially damaging inflammatory responses.

Original languageEnglish (US)
Pages (from-to)5429-5434
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number14
StatePublished - Apr 3 2012
Externally publishedYes


  • High-throughput screen
  • Placental
  • Surface plasmon resonance
  • Yeast two-hybrid

ASJC Scopus subject areas

  • General


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