Imaging

@article{,

title = {Structural Basis of Nanobody Recognition of Grapevine Fanleaf Virus and of Virus Resistance Loss},

author = {I Orlov and C Hemmer and L Ackerer and B Lorber and A Ghannam and V Poignavent and K Hleibieh and C Sauter and C Schmitt-Keichinger and L Belval and J M Hily and A Marmonier and V Komar and S Gersch and P Schellenberger and P Bron and E Vigne and S Muyldermans and O Lemaire and G Demangeat and C Ritzenthaler and B P Klaholz},

url = {https://www.ncbi.nlm.nih.gov/pubmed/32371486?dopt=Abstract},

doi = {10.1073/pnas.1913681117},

isbn = {32371486},

year  = {2020},

date = {2020-01-01},

journal = {Proc Natl Acad Sci U S A},

volume = {117},

number = {20},

pages = {10848-10855},

abstract = {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.},

keywords = {GFLV nanobody structural biology virus, SAUTER, Unité ARN},

pubstate = {published},

tppubtype = {article}

}