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Structure paper

TitleBroadly neutralizing antibodies to SARS-related viruses can be readily induced in rhesus macaques.
Journal, issue, pagesSci Transl Med, Vol. 14, Issue 657, Page eabl9605, Year 2022
Publish dateAug 10, 2022
AuthorsWan-Ting He / Meng Yuan / Sean Callaghan / Rami Musharrafieh / Ge Song / Murillo Silva / Nathan Beutler / Wen-Hsin Lee / Peter Yong / Jonathan L Torres / Mariane Melo / Panpan Zhou / Fangzhu Zhao / Xueyong Zhu / Linghang Peng / Deli Huang / Fabio Anzanello / James Ricketts / Mara Parren / Elijah Garcia / Melissa Ferguson / William Rinaldi / Stephen A Rawlings / David Nemazee / Davey M Smith / Bryan Briney / Yana Safonova / Thomas F Rogers / Jennifer M Dan / Zeli Zhang / Daniela Weiskopf / Alessandro Sette / Shane Crotty / Darrell J Irvine / Andrew B Ward / Ian A Wilson / Dennis R Burton / Raiees Andrabi /
PubMed AbstractTo prepare for future coronavirus (CoV) pandemics, it is desirable to generate vaccines capable of eliciting broadly neutralizing antibody responses to CoVs. Here, we show that immunization of ...To prepare for future coronavirus (CoV) pandemics, it is desirable to generate vaccines capable of eliciting broadly neutralizing antibody responses to CoVs. Here, we show that immunization of macaques with SARS-CoV-2 spike (S) protein with a two-shot protocol generated potent serum receptor binding domain cross-neutralizing antibody responses to both SARS-CoV-2 and SARS-CoV-1. Furthermore, responses were equally effective against most SARS-CoV-2 variants of concern (VOCs) and some were highly effective against Omicron. This result contrasts with human infection or many two-shot vaccination protocols where responses were typically more SARS-CoV-2 specific and where VOCs were less well neutralized. Structural studies showed that cloned macaque neutralizing antibodies, particularly using a given heavy chain germline gene, recognized a relatively conserved region proximal to the angiotensin converting enzyme 2 receptor binding site (RBS), whereas many frequently elicited human neutralizing antibodies targeted more variable epitopes overlapping the RBS. B cell repertoire differences between humans and macaques appeared to influence the vaccine response. The macaque neutralizing antibodies identified a pan-SARS-related virus epitope region less well targeted by human antibodies that could be exploited in rational vaccine design.
External linksSci Transl Med / PubMed:35947674 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.95 - 25.0 Å
Structure data

EMDB-26522: SARS-CoV-2 6P Mut7 in complex with K398.25 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26523: SARS-CoV-1 in complex with K398.25 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26524: SARS-CoV-2 6P Mut7 in complex with K398.16 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26525: SARS-CoV-2 6P Mut7 in complex with K398.16 Fab (3 bound)
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26526: SARS-CoV-1 in complex with K398.16 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26527: SARS-CoV-2 6P Mut7 in complex with K288.2 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26528: SARS-CoV-2 6P Mut7 in complex with K398.8 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26529: SARS-CoV-2 6P Mut7 in complex with K398.8 Fab (2 bound)
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26530: SARS-CoV-2 6P Mut7 in complex with K398.18 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26531: SARS-CoV-2 6P Mut7 in complex with K398.18 Fabs (2 bound)
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26532: SARS-CoV-2 6P Mut7 in complex with K398.22 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26533: SARS-CoV-2 6P Mut7 in complex with K398.22 Fab (2 bound)
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26534: SARS-CoV-1 in complex with K398.8 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26535: SARS-CoV-1 in complex with K398.8 Fab (2 bound)
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26536: SARS-CoV-1 in complex with K398.18 Fab (2 bound)
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26537: SARS-CoV-1 in complex with K398.18 Fab (3 bound)
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26538: SARS-CoV-1 in complex with K288.2 Fab
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-26539: SARS-CoV-1 in complex with K398.22 Fab
Method: EM (single particle) / Resolution: 25.0 Å

PDB-7tp3:
Crystal structure of SARS-CoV-2 receptor binding domain in complex with neutralizing antibody K288.2
Method: X-RAY DIFFRACTION / Resolution: 2.33 Å

PDB-7tp4:
Crystal structure of SARS-CoV-2 receptor binding domain in complex with neutralizing antibody K398.22
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-CAC:
CACODYLATE ION / Cacodylic acid

ChemComp-HOH:
WATER / Water

ChemComp-EDO:
1,2-ETHANEDIOL / Ethylene glycol

Source
  • severe acute respiratory syndrome coronavirus 2
  • macaca mulatta (Rhesus monkey)
  • Severe acute respiratory syndrome coronavirus
KeywordsIMMUNE SYSTEM / SARS-CoV-2 / antibody / neutralizing antibody / Fab / COVID-19 / coronavirus / receptor-binding domain / RBD / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex

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