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Structure paper

TitleAffinity-matured homotypic interactions induce spectrum of PfCSP structures that influence protection from malaria infection.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 4546, Year 2023
Publish dateJul 28, 2023
AuthorsGregory M Martin / Jonathan L Torres / Tossapol Pholcharee / David Oyen / Yevel Flores-Garcia / Grace Gibson / Re'em Moskovitz / Nathan Beutler / Diana D Jung / Jeffrey Copps / Wen-Hsin Lee / Gonzalo Gonzalez-Paez / Daniel Emerling / Randall S MacGill / Emily Locke / C Richter King / Fidel Zavala / Ian A Wilson / Andrew B Ward /
PubMed AbstractThe generation of high-quality antibody responses to Plasmodium falciparum (Pf) circumsporozoite protein (PfCSP), the primary surface antigen of Pf sporozoites, is paramount to the development of an ...The generation of high-quality antibody responses to Plasmodium falciparum (Pf) circumsporozoite protein (PfCSP), the primary surface antigen of Pf sporozoites, is paramount to the development of an effective malaria vaccine. Here we present an in-depth structural and functional analysis of a panel of potent antibodies encoded by the immunoglobulin heavy chain variable (IGHV) gene IGHV3-33, which is among the most prevalent and potent antibody families induced in the anti-PfCSP immune response and targets the Asn-Ala-Asn-Pro (NANP) repeat region. Cryo-electron microscopy (cryo-EM) reveals a remarkable spectrum of helical antibody-PfCSP structures stabilized by homotypic interactions between tightly packed fragments antigen binding (Fabs), many of which correlate with somatic hypermutation. We demonstrate a key role of these mutated homotypic contacts for high avidity binding to PfCSP and in protection from Pf malaria infection. Together, these data emphasize the importance of anti-homotypic affinity maturation in the frequent selection of IGHV3-33 antibodies and highlight key features underlying the potent protection of this antibody family.
External linksNat Commun / PubMed:37507365 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.9 - 3.84 Å
Structure data

27781

8dyt

EMDB-27781, PDB-8dyt:
Cryo-EM structure of 227 Fab in complex with (NPNA)8 peptide
Method: EM (single particle) / Resolution: 3.3 Å

27784

8dyw

EMDB-27784, PDB-8dyw:
Cryo-EM structure of 239 Fab in complex with recombinant shortened Plasmodium falciparum circumsporozoite protein (rsCSP)
Method: EM (single particle) / Resolution: 3.72 Å

27785

8dyx

EMDB-27785, PDB-8dyx:
Cryo-EM structure of 311 Fab in complex with recombinant shortened Plasmodium falciparum circumsporozoite protein (rsCSP)
Method: EM (single particle) / Resolution: 3.0 Å

27786

8dyy

EMDB-27786, PDB-8dyy:
Cryo-EM structure of 334 Fab in complex with recombinant shortened Plasmodium falciparum circumsporozoite protein (rsCSP)
Method: EM (single particle) / Resolution: 3.62 Å

27787

8dz3

EMDB-27787, PDB-8dz3:
Cryo-EM structure of 337 Fab in complex with recombinant shortened Plasmodium falciparum circumsporozoite protein (rsCSP)
Method: EM (single particle) / Resolution: 2.7 Å

27788

8dz4

EMDB-27788, PDB-8dz4:
Cryo-EM structure of 356 Fab in complex with recombinant shortened Plasmodium falciparum circumsporozoite protein (rsCSP)
Method: EM (single particle) / Resolution: 3.2 Å

27789

8dz5

EMDB-27789, PDB-8dz5:
Cryo-EM structure of 364 Fab in complex with recombinant shortened Plasmodium falciparum circumsporozoite protein (rsCSP)
Method: EM (single particle) / Resolution: 3.84 Å

PDB-8ekf:
X-ray crystal structure of 311R Fab in complex with the PfCSP peptide NPNA-3
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • plasmodium falciparum (malaria parasite P. falciparum)
  • homo sapiens (human)
  • plasmodium falciparum 3d7 (eukaryote)
  • Escherichia coli (E. coli)
KeywordsIMMUNE SYSTEM / malaria antibody / PfCSP / Antibody / Antigen / Malaria

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