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TitleConserved fiber-penton base interaction revealed by nearly atomic resolution cryo-electron microscopy of the structure of adenovirus provides insight into receptor interaction.
Journal, issue, pagesJ Virol, Vol. 86, Issue 22, Page 12322-12329, Year 2012
Publish dateSep 5, 2012
AuthorsChangchun Cao / Xiaoyan Dong / Xiaobing Wu / Boyun Wen / Gang Ji / Lingpeng Cheng / Hongrong Liu /
PubMed AbstractAdenovirus (Ad) cell attachment is initiated by the attachment of the fiber protein to a primary receptor (usually CAR or CD46). This event is followed by the engagement of the penton base protein ...Adenovirus (Ad) cell attachment is initiated by the attachment of the fiber protein to a primary receptor (usually CAR or CD46). This event is followed by the engagement of the penton base protein with a secondary receptor (integrin) via its loop region, which contains an Arg-Gly-Asp (RGD) motif, to trigger virus internalization. To understand the well-orchestrated adenovirus cell attachment process that involves the fiber and the penton base, we reconstructed the structure of an Ad5F35 capsid, comprising an adenovirus type 5 (Ad5) capsid pseudotyped with an Ad35 fiber, at a resolution of approximately 4.2 Å. The fiber-penton base interaction in the cryo-electron microscopic (cryo-EM) structure of Ad5F35 is similar to that in the cryo-EM structure of Ad5, indicating that the fiber-penton base interaction of adenovirus is conserved. Our structure also confirms that the C-terminal segment of the fiber tail domain constitutes the bottom trunk of the fiber shaft. Based on the conserved fiber-penton base interaction, we have proposed a model for the interaction of Ad5F35 with its primary and secondary receptors. This model could provide insight for designing adenovirus gene delivery vectors.
External linksJ Virol / PubMed:22951835 / PubMed Central
MethodsEM (single particle)
Resolution4.2 - 7.0 Å
Structure data

EMDB-5454:
7 Angstrom resolution cryo-EM map of Ad5F35
Method: EM (single particle) / Resolution: 7.0 Å

EMDB-5467:
4.2 Angstrom Cryo-EM structure of Ad5F35
Method: EM (single particle) / Resolution: 4.2 Å

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