KAHRP

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

Knob-associated histidine-rich protein
Identifiers
OrganismPlasmodium falciparum
Symbol?
UniProtP09346
EMP3-KAHRP-like N-terminal domain
Identifiers
SymbolEKAL
PfamPF17986
InterProIPR040805
EMP3 refers to "Erythrocyte membrane protein 3." It is likely a misnomer, as no reported PfEMP3 sequences contain this domain. PfEMP3 is arranged next to KAHRP in the P. falciparum genome, a probable cause of misidentification.

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. PMID 19369950.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.
  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.CS1 maint: multiple names: authors list (link)


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