+検索条件
-Structure paper
タイトル | High flavivirus structural plasticity demonstrated by a non-spherical morphological variant. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 3112, Year 2020 |
掲載日 | 2020年6月19日 |
著者 | Seamus R Morrone / Valerie S Y Chew / Xin-Ni Lim / Thiam-Seng Ng / Victor A Kostyuchenko / Shuijun Zhang / Melissa Wirawan / Pau-Ling Chew / Jaime Lee / Joanne L Tan / Jiaqi Wang / Ter Yong Tan / Jian Shi / Gavin Screaton / Marc C Morais / Shee-Mei Lok / |
PubMed 要旨 | Previous flavivirus (dengue and Zika viruses) studies showed largely spherical particles either with smooth or bumpy surfaces. Here, we demonstrate flavivirus particles have high structural ...Previous flavivirus (dengue and Zika viruses) studies showed largely spherical particles either with smooth or bumpy surfaces. Here, we demonstrate flavivirus particles have high structural plasticity by the induction of a non-spherical morphology at elevated temperatures: the club-shaped particle (clubSP), which contains a cylindrical tail and a disc-like head. Complex formation of DENV and ZIKV with Fab C10 stabilize the viruses allowing cryoEM structural determination to ~10 Å resolution. The caterpillar-shaped (catSP) Fab C10:ZIKV complex shows Fabs locking the E protein raft structure containing three E dimers. However, compared to the original spherical structure, the rafts have rotated relative to each other. The helical tail structure of Fab C10:DENV3 clubSP showed although the Fab locked an E protein dimer, the dimers have shifted laterally. Morphological diversity, including clubSP and the previously identified bumpy and smooth-surfaced spherical particles, may help flavivirus survival and immune evasion. |
リンク | Nat Commun / PubMed:32561757 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 9.4 - 10.4 Å |
構造データ | EMDB-30278, PDB-7c2s: EMDB-30279, PDB-7c2t: |
由来 |
|
キーワード | VIRUS / antibody / neutralization |