title: Solid-to-fluid DNA transition inside HSV-1 capsid close to the temperature of infection.
abstract: DNA in the human Herpes simplex virus type 1 (HSV-1) capsid is packaged to a tight density. This leads to tens of atmospheres of internal pressure responsible for the delivery of the herpes genome into the cell nucleus. In this study we show that, despite its liquid crystalline state inside the capsid, the DNA is fluid-like, which facilitates its ejection into the cell nucleus during infection. We found that the sliding friction between closely packaged DNA strands, caused by interstrand repulsive interactions, is reduced by the ionic environment of epithelial cells and neurons susceptible to herpes infection. However, variations in the ionic conditions corresponding to neuronal activity can restrict DNA mobility in the capsid, making it more solid-like. This can inhibit intranuclear DNA release and interfere with viral replication. In addition, the temperature of the human host (37 °C) induces a disordering transition of the encapsidated herpes genome, which reduces interstrand interactions and provides genome mobility required for infection.
authors.affiliation: 1] Carnegie Mellon University, Department of Physics, Pittsburgh, Pennsylvania, USA. [2].
authors.forename: Udom
authors.initials: U
authors.lastname: Sae-Ueng
authors.affiliation: 1] Carnegie Mellon University, Department of Physics, Pittsburgh, Pennsylvania, USA. [2].
authors.forename: Dong
authors.initials: D
authors.lastname: Li
authors.affiliation: X-ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois, USA.
authors.forename: Xiaobing
authors.initials: X
authors.lastname: Zuo
authors.affiliation: Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
authors.forename: Jamie B
authors.initials: JB
authors.lastname: Huffman
authors.affiliation: Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
authors.forename: Fred L
authors.initials: FL
authors.lastname: Homa
authors.affiliation: Laboratory of Physical and Structural Biology, Program in Physical Biology, National Institutes of Health, Bethesda, Maryland, USA.
authors.forename: Donald
authors.initials: D
authors.lastname: Rau
authors.affiliation: 1] Carnegie Mellon University, Department of Physics, Pittsburgh, Pennsylvania, USA. [2] Lund University, Department of Biochemistry and Structural Biology, Lund, Sweden.
authors.forename: Alex
authors.initials: A
authors.lastname: Evilevitch
mesh_terms: D000818:Animals; D002213:Capsid / Q000737:chemistry*; D002467:Cell Nucleus / Q000821:virology*; D002522:Chlorocebus aethiops; D004279:DNA, Viral / Q000737:chemistry*; D016679:Genome, Viral; D018259:Herpesvirus 1, Human / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D007700:Kinetics; D009690:Nucleic Acid Conformation; D044367:Phase Transition; D013696:Temperature; D014709:Vero Cells; D014779:Virus Replication
chemical_list: D004279:DNA, Viral