Plasmodium falciparum merozoite surface protein 1 blocks the proinflammatory protein S100P.

نویسندگان

  • 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
چکیده

The malaria parasite, Plasmodium falciparum, 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. Here we show that 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 in monocytes 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.

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عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 109 14  شماره 

صفحات  -

تاریخ انتشار 2012