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Structure paper

TitleA stabilized tandem antigen chimera that elicits potent malaria transmission-reducing activity.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateJan 24, 2026
AuthorsDanton Ivanochko / Kazutoyo Miura / Sophia Hailemariam / Rashmi Ravichandran / Yiting Song / Wei-Chiao Huang / Rianne Stoter / Karina Teelen / Geert-Jan van Gemert / Elizabeth M Leaf / Sidney Chan / Christine Men / Anthony Semesi / Carol Shiu / Randall S MacGill / Carole A Long / Matthijs M Jore / Neil P King / Jonathan F Lovell / Jean-Philippe Julien /
PubMed AbstractMalaria parasite transmission remains a barrier to elimination since asymptomatic individuals sustain the infectious reservoir. Transmission-blocking vaccine (TBV) candidates targeting Plasmodium ...Malaria parasite transmission remains a barrier to elimination since asymptomatic individuals sustain the infectious reservoir. Transmission-blocking vaccine (TBV) candidates targeting Plasmodium falciparum (Pf) gametocyte surface proteins Pfs230 and Pfs48/45 have shown promise in clinical trials. Several vaccine candidates have been developed for these antigens, yet it is unclear which elicit the most robust and durable transmission-blocking responses. From structure-function relationships of monoclonal antibodies in complex with both antigens, we report the development of a stabilized tandem antigen chimera (STAC), which presents the most potent epitopes from Pfs230 domain 1 (Pfs230-D1) and Pfs48/45 domain 3 (Pfs48/45-D3) in a single construct, while masking non-functional epitopes using an engineered pseudo-native domain disposition. Iterative structure-guided optimization improved antigen yields and stability, while nanoparticle-based multimerization enhanced the functional transmission-reducing activity elicited by the immunogen in female mice. Immunizations with STAC genetically conjugated to self-assembling protein nanoparticles elicited antibodies with potent transmission-reducing activity comparable or superior to the multimerized Pfs230-D1 and Pfs48/45-D3. These findings establish STAC as a promising next-generation TBV candidate to disrupt malaria transmission and accelerate elimination efforts. More broadly, our results support the engineering of highly ordered and stable multi-domain antigens in a single protein as a strategy for the cost-efficient development of multi-component vaccines.
External linksNat Commun / PubMed:41580424 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.85 - 3.22 Å
Structure data

49130

9n8j

EMDB-49130, PDB-9n8j:
Stabilized tandem antigen chimera of Pfs230 and Pfs48/45 bound by potent mAbs
Method: EM (single particle) / Resolution: 3.22 Å

PDB-9n8i:
Pfs230 domain 1 bound by RUPA-39 Fab
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-9n8n:
Tandem antigen chimera of Pfs230 and Pfs48/45 bound by potent mAbs
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-CL:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-ACT:
ACETATE ION

ChemComp-CAC:
CACODYLATE ION

Source
  • homo sapiens (human)
  • rattus (rats)
  • plasmodium falciparum (malaria parasite P. falciparum)
  • plasmodium falciparum 3d7 (eukaryote)
  • lama glama (llama)
KeywordsIMMUNE SYSTEM / Antibody / Malaria / Pfs230 / Pfs48/45 / structure-based immunogen design / human transmission-blocking antibodies / Malaria vaccine

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