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KAHRP

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KAHRP (Plasmodium falciparum knob-associated histidine-rich protein) is a protein expressed in erythrocytes infected by Plasmodium falciparum. KAHRP is a major component of knobs, feature found on Plasmodium falciparum infected erythrocytes.

It has been suggested that KAHRP may play a role in trafficking or docking PfEMP1, major malarial cytoadherence protein to the erythrocyte membrane;[1] however, these findings were disputed by recent NMR and fluorescence anisotropy studies showing no interaction between PfEMP1 and KAHRP.[2]

Instead, KAHRP was shown to interact with Ankyrin, more precisely the D3 subunit of the Membrane-binding domain of Ankyrin type 1.[3] This interaction was suggested via SPR, ELISA, and Pulldown studies, however, it has not been confirmed by NMR, ITC, crystallography, or fluorescence anisotropy.

References

  1. ^ Alexander G. Maier, Brian M. Cooke, Alan F. Cowman & Leann Tilley (May 2009). "Malaria parasite proteins that remodel the host erythrocyte : Abstract". Nature Reviews Microbiology. 7 (5): 341–354. doi:10.1038/nrmicro2110. Retrieved 2014-03-15.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Christina Mayer; Leanne Slater; Michele C. Erat; Robert Konrat; Ioannis Vakonakis (March 2, 2012). "Structural Analysis of the Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) Intracellular Domain Reveals a Conserved Interaction Epitope". J Biol Chem. 287 (10): 7182–7189. doi:10.1074/jbc.M111.330779. PMC 3293552. PMID 22249178.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  3. ^ Weng H1, Guo X, Papoin J, Wang J, Coppel R, Mohandas N, An X. (January 24, 2014). "Interaction of Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) with erythrocyte ankyrin R is required for its attachment to the erythrocyte membrane". Biochim Biophys Acta. 1838 (1 Pt B): 185–192. doi:10.1016/j.bbamem.2013.09.014. PMC 4403245. PMID 24090929.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: numeric names: authors list (link)