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TitleUnexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.
Journal, issue, pagesCell, Vol. 176, Issue 5, Page 1026-1039.e15, Year 2019
Publish dateFeb 21, 2019
AuthorsAlexandra C Walls / Xiaoli Xiong / Young-Jun Park / M Alejandra Tortorici / Joost Snijder / Joel Quispe / Elisabetta Cameroni / Robin Gopal / Mian Dai / Antonio Lanzavecchia / Maria Zambon / Félix A Rey / Davide Corti / David Veesler /
PubMed AbstractRecent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways ...Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism.
External linksCell / PubMed:30712865 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.5 - 4.5 Å
Structure data

0401

6nb3

EMDB-0401, PDB-6nb3:
MERS-CoV complex with human neutralizing LCA60 antibody Fab fragment (state 1)
Method: EM (single particle) / Resolution: 3.5 Å

0402

6nb4

EMDB-0402, PDB-6nb4:
MERS-CoV S complex with human neutralizing LCA60 antibody Fab fragment (state 2)
Method: EM (single particle) / Resolution: 3.6 Å

0403

6nb6

EMDB-0403, PDB-6nb6:
SARS-CoV complex with human neutralizing S230 antibody Fab fragment (state 1)
Method: EM (single particle) / Resolution: 4.2 Å

0404

6nb7

EMDB-0404, PDB-6nb7:
SARS-CoV complex with human neutralizing S230 antibody Fab fragment (state 2)
Method: EM (single particle) / Resolution: 4.5 Å

PDB-6nb5:
Crystal structure of anti- MERS-CoV human neutralizing LCA60 antibody Fab fragment
Method: X-RAY DIFFRACTION / Resolution: 3.0 Å

PDB-6nb8:
Crystal structure of anti- SARS-CoV human neutralizing S230 antibody Fab fragment
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-HOH:
WATER / Water

Source
  • middle east respiratory syndrome coronavirus
  • middle east respiratory syndrome-related coronavirus
  • homo sapiens (human)
  • sars coronavirus
KeywordsVIRUS / coronavirus spike glycoprotein / MERS-CoV / SARS-CoV / human neutralizing antibodies / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / IMMUNE SYSTEM / Fab / Coronavirus / Glycoprotein / SARS

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