Journal
STRUCTURE
Volume 25, Issue 10, Pages 1562-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2017.08.007
Keywords
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Funding
- Spanish Adenovirus Network (AdenoNet) [BIO201568990-REDT]
- Spanish Interdisciplinary Network on the Biophysics of Viruses (Biofivinet) [FIS2011-16090-E]
- Spanish Ministry of Economy and Competitiveness [BFU2011-24843, BFU2014-53425-P, BFU2013-41249-P, FIS2011-16090-E, BIO2015-68990-REDT]
- Spanish Agencia Estatal de Investigacion [BFU2016-74868-P]
- European Regional Development Fund
- Instituto de Salud Carlos III of Spain
- CSIC-VAST
- La Caixa
- EMBO
- Spanish MICINN-German DAAD [DE2009-0019]
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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 crystal-lography 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 beta 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.
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