Reticulocyte binding protein homologs

Reticulocyte binding protein homologs (RHs) are a superfamily of proteins found in Plasmodium responsible for cell invasion. Together with the family of erythrocyte binding-like proteins (EBLs) they make up the two families of invasion proteins universal to Plasmodium.[1] The two families function cooperatively.[2]

Plasmodium falciparum reticulocyte-binding protein homolog 5 (RH5), coiled-coil domain
Identifiers
SymbolRf5
PfamPF18515
InterProIPR041668

This family is named after the reticulocyte binding proteins in P. vivax, a parasite that only infects reticulocytes (immature red blood cells) expressing the Duffy antigen. Homologs have since been identified in P. yoelii and P. reichenowi.[1] A P. falciparum protein complex called PfRH5-PfCyRPA-PfRipr (RCR) is known to bind basigin, has its structure known, and is a potential vaccine target.[3] PfRH4 is known to bind complement receptor 1.[4]

RHs do not express any significant sequence feature for specific domains, except for a set of transmembrane helices at the C-terminal. From experimentation on partial proteins, RHs are known to contain enterocyte-binding and nucleotide-sensing domains (EBD and NBD) that may partially overlap. The structure of the EBD has been experimentally observed in 2011 by small angle X-ray scattering.[5] A much better crystal structure for an N-terminal receptor-binding domain (presumably the same as EBD) was published in 2014.[4]

References
  1. Iyer, Jayasree; Grüner, Anne Charlotte; Rénia, Laurent; Snounou, Georges; Preiser, Peter R. (July 2007). "Invasion of host cells by malaria parasites: a tale of two protein families". Molecular Microbiology. 65 (2): 231–249. doi:10.1111/j.1365-2958.2007.05791.x. PMID 17630968.
  2. Lopaticki, Sash; Maier, Alexander G.; Thompson, Jennifer; Wilson, Danny W.; Tham, Wai-Hong; Triglia, Tony; Gout, Alex; Speed, Terence P.; Beeson, James G.; Healer, Julie; Cowman, Alan F.; Adams, J. H. (March 2011). "Reticulocyte and Erythrocyte Binding-Like Proteins Function Cooperatively in Invasion of Human Erythrocytes by Malaria Parasites". Infection and Immunity. 79 (3): 1107–1117. doi:10.1128/IAI.01021-10. PMC 3067488. PMID 21149582.
  3. Ragotte, Robert J.; Higgins, Matthew K.; Draper, Simon J. (June 2020). "The RH5-CyRPA-Ripr Complex as a Malaria Vaccine Target". Trends in Parasitology. 36 (6): 545–559. doi:10.1016/j.pt.2020.04.003. PMC 7246332.
  4. Wright, Katherine E.; Hjerrild, Kathryn A.; Bartlett, Jonathan; Douglas, Alexander D.; Jin, Jing; Brown, Rebecca E.; Illingworth, Joseph J.; Ashfield, Rebecca; Clemmensen, Stine B.; de Jongh, Willem A.; Draper, Simon J.; Higgins, Matthew K. (17 August 2014). "Structure of malaria invasion protein RH5 with erythrocyte basigin and blocking antibodies". Nature. 515 (7527): 427–430. doi:10.1038/nature13715.
  5. Grüber, Ardina; Gunalan, Karthigayan; Ramalingam, Jeya Kumar; Manimekalai, Malathy S. S.; Grüber, Gerhard; Preiser, Peter R.; Adams, J. H. (July 2011). "Structural Characterization of the Erythrocyte Binding Domain of the Reticulocyte Binding Protein Homologue Family of Plasmodium yoelii". Infection and Immunity. 79 (7): 2880–2888. doi:10.1128/IAI.01326-10. PMC 3191949. PMID 21482683.
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