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TitleStructural basis for antibody recognition of the NANP repeats in circumsporozoite protein.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 114, Issue 48, Page E10438-E10445, Year 2017
Publish dateNov 28, 2017
AuthorsDavid Oyen / Jonathan L Torres / Ulrike Wille-Reece / Christian F Ockenhouse / Daniel Emerling / Jacob Glanville / Wayne Volkmuth / Yevel Flores-Garcia / Fidel Zavala / Andrew B Ward / C Richter King / Ian A Wilson /
PubMed AbstractAcquired resistance against antimalarial drugs has further increased the need for an effective malaria vaccine. The current leading candidate, RTS,S, is a recombinant circumsporozoite protein (CSP)- ...Acquired resistance against antimalarial drugs has further increased the need for an effective malaria vaccine. The current leading candidate, RTS,S, is a recombinant circumsporozoite protein (CSP)-based vaccine against that contains 19 NANP repeats followed by a thrombospondin repeat domain. Although RTS,S has undergone extensive clinical testing and has progressed through phase III clinical trials, continued efforts are underway to enhance its efficacy and duration of protection. Here, we determined that two monoclonal antibodies (mAbs 311 and 317), isolated from a recent controlled human malaria infection trial exploring a delayed fractional dose, inhibit parasite development in vivo by at least 97%. Crystal structures of antibody fragments (Fabs) 311 and 317 with an (NPNA) peptide illustrate their different binding modes. Notwithstanding, one and three of the three NPNA repeats adopt similar well-defined type I β-turns with Fab311 and Fab317, respectively. Furthermore, to explore antibody binding in the context of CSP, we used negative-stain electron microscopy on a recombinant shortened CSP (rsCSP) construct saturated with Fabs. Both complexes display a compact rsCSP with multiple Fabs bound, with the rsCSP-Fab311 complex forming a highly organized helical structure. Together, these structural insights may aid in the design of a next-generation malaria vaccine.
External linksProc Natl Acad Sci U S A / PubMed:29138320 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.103 - 25.0 Å
Structure data

EMDB-7068:
rsCSP + Fab311 Complex
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-7069:
rsCSP + Fab317 Complex
Method: EM (single particle) / Resolution: 25.0 Å

PDB-6axk:
Crystal structure of Fab311 complex
Method: X-RAY DIFFRACTION / Resolution: 2.103 Å

PDB-6axl:
Crystal structure of Fab317 complex
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • plasmodium falciparum (malaria parasite P. falciparum)
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / Fab fragment

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