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TitleAnalysis of monoclonal antibodies against the malaria invasion complex protein RIPR reveals the structural basis for synergistic antibody protection.
Journal, issue, pagesImmunity, Year 2026
Publish dateJun 12, 2026
AuthorsBarnabas G Williams / Jordan R Barrett / Josefin Bartholdson Scott / Cassandra A Rigby / Matteo Cagiada / Doris Quinkert / Kirsty McHugh / Anna Huhn / Sean A Burnap / Camille Gourjault / Francesca Byrne / Sai Sundar Rajan Raghavan / Ana Rodrigues / Laura Bergamaschi / Beatrice Balzarotti / Simon Watson / Noah Miller / Lloyd D W King / Francesca R Donnellan / Camilla A Gladstone / Jemima Paterson / Stefania Scalabrino / Sarah E Silk / Jo Salkeld / Angela M Minassian / Katherine Skinner / Weston B Struwe / Charlotte M Deane / Stephen T Reece / Andrew B Ward / Simon J Draper /
PubMed AbstractPlasmodium falciparum RH5-interacting protein (RIPR) is central to the essential PTRAMP-CSS-RIPR-CyRPA-RH5 (PCRCR) complex, a leading target of blood-stage malaria vaccines. However, mechanisms ...Plasmodium falciparum RH5-interacting protein (RIPR) is central to the essential PTRAMP-CSS-RIPR-CyRPA-RH5 (PCRCR) complex, a leading target of blood-stage malaria vaccines. However, mechanisms whereby anti-RIPR antibodies inhibit parasite invasion are poorly understood. We characterized 83 human IgG monoclonal antibodies (mAbs) from RIPR-vaccinated Kymouse platform mice. Single mAbs had minimal neutralizing activity; however, high-level synergistic inhibition was observed with pools of mAbs targeting the RIPR-tail region. Structural characterization and molecular dynamics simulations of RIPR-tail showed that mAbs targeting epidermal growth factor (EGF)-like domains 6-8 (RIPR), but not RIPR or the C-terminal domain (RIPR), synergized to constrain the RIPR-tail conformation. The same antibodies dissociated PTRAMP-CSS from RIPR, thereby enabling anti-RIPR mAbs or anti-CSS single-domain Abs to bind and potentiate anti-RIPR IgG. Addition of these mAbs to IgG from humans immunized with the R78C (RIPR-CyRPA) candidate vaccine enhanced malaria growth inhibition. These data provide a framework to guide next-generation blood-stage malaria vaccine design.
External linksImmunity / PubMed:42285102
MethodsEM (single particle)
Resolution2.97 - 4.01 Å
Structure data

72260

9q69

EMDB-72260, PDB-9q69:
Cryo-electron microscopy structure of PfRIPR bound to monoclonal antibodies RP.047, RP.057 and RP.035
Method: EM (single particle) / Resolution: 3.35 Å

72265

9q6b

EMDB-72265, PDB-9q6b:
Cryo-electron microscopy structure of PfRIPR bound to monoclonal antibodies RP.093, RP.073 and RP.063
Method: EM (single particle) / Resolution: 2.97 Å

72294

9q7c

EMDB-72294, PDB-9q7c:
Cryo-electron microscopy structure of PfRIPR bound to monoclonal antibodies RP.092 and RP.052
Method: EM (single particle) / Resolution: 4.01 Å

Source
  • mus musculus (house mouse)
  • plasmodium falciparum 3d7 (eukaryote)
KeywordsIMMUNE SYSTEM / Malaria / RIPR / Monoclonal antibodies / Vaccine / Invasion complex / Plasmodium falciparum

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