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Title: Adenovirus major core protein condenses DNA in clusters and bundles, modulating genome release and capsid internal pressure
Author: Martín-González, Natalia
Hernando-Pérez, Mercedes
Condezo, Gabriela N.
Pérez-Illana, Marta
Siber, Antonio
Reguera, D. (David)
Ostapchuk, Philomena
Hearing, Patrick
San Martín, Carmen
de Pablo, Pedro J.
Keywords: Virus ADN
DNA viruses
Issue Date: 26-Sep-2019
Publisher: Oxford University Press
Abstract: Some viruses package dsDNA together with large amounts of positively charged proteins, thought to help condense the genome inside the capsid with no evidence. Further, this role is not clear because these viruses have typically lower packing fractions than viruses encapsidating naked dsDNA. In addition, it has recently been shown that the major adenovirus condensing protein (polypeptide VII) is dispensable for genome encapsidation. Here, we study the morphology and mechanics of adenovirus particles with (Ad5-wt) and without (Ad5-VII-) protein VII. Ad5-VII- particles are stiffer than Ad5-wt, but DNA-counterions revert this difference, indicating that VII screens repulsive DNA-DNA interactions. Consequently, its absence results in increased internal pressure. The core is slightly more ordered in the absence of VII and diffuses faster out of Ad5-VII- than Ad5-wt fractured particles. In Ad5-wt unpacked cores, dsDNA associates in bundles interspersed with VII-DNA clusters. These results indicate that protein VII condenses the adenovirus genome by combining direct clustering and promotion of bridging by other core proteins. This condensation modulates the virion internal pressure and DNA release from disrupted particles, which could be crucial to keep the genome protected inside the semi-disrupted capsid while traveling to the nuclear pore.
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It is part of: Nucleic Acids Research, 2019, vol. 47, num. 17, p. 9231-9242
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ISSN: 0305-1048
Appears in Collections:Articles publicats en revistes (Física de la Matèria Condensada)

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