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TitleStructural basis of nanobody recognition of grapevine fanleaf virus and of virus resistance loss.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 20, Page 10848-10855, Year 2020
Publish dateMay 19, 2020
AuthorsIgor Orlov / Caroline Hemmer / Léa Ackerer / Bernard Lorber / Ahmed Ghannam / Vianney Poignavent / Kamal Hleibieh / Claude Sauter / Corinne Schmitt-Keichinger / Lorène Belval / Jean-Michel Hily / Aurélie Marmonier / Véronique Komar / Sophie Gersch / Pascale Schellenberger / Patrick Bron / Emmanuelle Vigne / Serge Muyldermans / Olivier Lemaire / Gérard Demangeat / Christophe Ritzenthaler / Bruno P Klaholz /
PubMed AbstractGrapevine fanleaf virus (GFLV) is a picorna-like plant virus transmitted by nematodes that affects vineyards worldwide. Nanobody (Nb)-mediated resistance against GFLV has been created recently, and ...Grapevine fanleaf virus (GFLV) is a picorna-like plant virus transmitted by nematodes that affects vineyards worldwide. Nanobody (Nb)-mediated resistance against GFLV has been created recently, and shown to be highly effective in plants, including grapevine, but the underlying mechanism is unknown. Here we present the high-resolution cryo electron microscopy structure of the GFLV-Nb23 complex, which provides the basis for molecular recognition by the Nb. The structure reveals a composite binding site bridging over three domains of one capsid protein (CP) monomer. The structure provides a precise mapping of the Nb23 epitope on the GFLV capsid in which the antigen loop is accommodated through an induced-fit mechanism. Moreover, we uncover and characterize several resistance-breaking GFLV isolates with amino acids mapping within this epitope, including C-terminal extensions of the CP, which would sterically interfere with Nb binding. Escape variants with such extended CP fail to be transmitted by nematodes linking Nb-mediated resistance to vector transmission. Together, these data provide insights into the molecular mechanism of Nb23-mediated recognition of GFLV and of virus resistance loss.
External linksProc Natl Acad Sci U S A / PubMed:32371486 / PubMed Central
MethodsEM (single particle)
Resolution2.8 Å
Structure data

PDB-5foj:
Cryo electron microscopy structure of Grapevine Fanleaf Virus complex with Nanobody
Method: ELECTRON MICROSCOPY / Resolution: 2.8 Å

Source
  • camelus dromedarius (Arabian camel)
  • grapevine fanleaf virus
KeywordsVIRUS / NANOBODY / COMPLEX

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