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-Structure paper
タイトル | Structure of a Reptilian Adenovirus Reveals a Phage Tailspike Fold Stabilizing a Vertebrate Virus Capsid. |
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ジャーナル・号・ページ | Structure, Vol. 25, Issue 10, Page 1562-11573.e5, Year 2017 |
掲載日 | 2017年10月3日 |
著者 | Rosa Menéndez-Conejero / Thanh H Nguyen / Abhimanyu K Singh / Gabriela N Condezo / Rachel E Marschang / Mark J van Raaij / Carmen San Martín / |
PubMed 要旨 | Although non-human adenoviruses (AdVs) might offer solutions to problems posed by human AdVs as therapeutic vectors, little is known about their basic biology. In particular, there are no structural ...Although non-human adenoviruses (AdVs) might offer solutions to problems posed by human AdVs as therapeutic vectors, little is known about their basic biology. In particular, there are no structural studies on the complete virion of any AdV with a non-mammalian host. We combine mass spectrometry, cryo-electron microscopy, and protein crystallography to characterize the composition and structure of a snake AdV (SnAdV-1, Atadenovirus genus). SnAdV-1 particles contain the genus-specific proteins LH3, p32k, and LH2, a previously unrecognized structural component. Remarkably, the cementing protein LH3 has a trimeric β helix fold typical of bacteriophage host attachment proteins. The organization of minor coat proteins differs from that in human AdVs, correlating with higher thermostability in SnAdV-1. These findings add a new piece to the intriguing puzzle of virus evolution, hint at the use of cell entry pathways different from those in human AdVs, and will help development of new, thermostable SnAdV-1-based vectors. |
リンク | Structure / PubMed:28943338 |
手法 | EM (単粒子) / X線回折 |
解像度 | 2 - 10.9 Å |
構造データ | EMDB-3599: PDB-5g5n: PDB-5g5o: |
化合物 | ChemComp-GOL: ChemComp-MMC: ChemComp-CL: ChemComp-HOH: ChemComp-ACT: |
由来 |
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キーワード | VIRAL PROTEIN / CAPSID PROTEIN / BETA-HELIX |