5foj
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/POL2_GFLV POL2_GFLV]] Protein 2A: implicated in RNA2 replication. Could also be required for nematode transmission of the virus. Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids. | [[http://www.uniprot.org/uniprot/POL2_GFLV POL2_GFLV]] Protein 2A: implicated in RNA2 replication. Could also be required for nematode transmission of the virus. Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
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| + | Structural basis of nanobody recognition of grapevine fanleaf virus and of virus resistance loss.,Orlov I, Hemmer C, Ackerer L, Lorber B, Ghannam A, Poignavent V, Hleibieh K, Sauter C, Schmitt-Keichinger C, Belval L, Hily JM, Marmonier A, Komar V, Gersch S, Schellenberger P, Bron P, Vigne E, Muyldermans S, Lemaire O, Demangeat G, Ritzenthaler C, Klaholz BP Proc Natl Acad Sci U S A. 2020 May 5. pii: 1913681117. doi:, 10.1073/pnas.1913681117. PMID:32371486<ref>PMID:32371486</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5foj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
Revision as of 05:54, 20 May 2020
Cryo electron microscopy structure of Grapevine Fanleaf Virus complex with Nanobody
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Categories: Arabian camel | Grapevine fanleaf virus | Large Structures | Ackerer, L | Belval, L | Bron, P | Demangeat, G | Gersch, S | Ghannam, A | Hemmer, C | Hily, J M | Hleibieh, K | Klaholz, B P | Komar, V | Lemaire, O | Lorber, B | Marmonier, A | Muyldermans, S | Orlov, I | Poignavent, V | Ritzenthaler, C | Sauter, C | Schellenberger, P | Schmitt-Keichinger, C | Vigne, E | Complex | Nanobody | Virus
