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Full-Text Articles in Medicine and Health Sciences
Terminase Subunits From The Pseudomonas-Phage E217, Ravi K Lokareddy, Chun-Feng David Hou, Steven G Doll, Fenglin Li, Richard E Gillilan, Francesca Forti, David S Horner, Federica Briani, Gino Cingolani
Terminase Subunits From The Pseudomonas-Phage E217, Ravi K Lokareddy, Chun-Feng David Hou, Steven G Doll, Fenglin Li, Richard E Gillilan, Francesca Forti, David S Horner, Federica Briani, Gino Cingolani
Department of Biochemistry and Molecular Biology Faculty Papers
Pseudomonas phages are increasingly important biomedicines for phage therapy, but little is known about how these viruses package DNA. This paper explores the terminase subunits from the Myoviridae E217, a Pseudomonas-phage used in an experimental cocktail to eradicate P. aeruginosa in vitro and in animal models. We identified the large (TerL) and small (TerS) terminase subunits in two genes ∼58 kbs away from each other in the E217 genome. TerL presents a classical two-domain architecture, consisting of an N-terminal ATPase and C-terminal nuclease domain arranged into a bean-shaped tertiary structure. A 2.05 Å crystal structure of the C-terminal domain revealed …
Viral Small Terminase: A Divergent Structural Framework For A Conserved Biological Function., Ravi K. Lokareddy, Chun-Feng David Hou, Fenglin Li, Ruoyu Yang, Gino Cingolani
Viral Small Terminase: A Divergent Structural Framework For A Conserved Biological Function., Ravi K. Lokareddy, Chun-Feng David Hou, Fenglin Li, Ruoyu Yang, Gino Cingolani
Department of Biochemistry and Molecular Biology Faculty Papers
The genome packaging motor of bacteriophages and herpesviruses is built by two terminase subunits, known as large (TerL) and small (TerS), both essential for viral genome packaging. TerL structure, composition, and assembly to an empty capsid, as well as the mechanisms of ATP-dependent DNA packaging, have been studied in depth, shedding light on the chemo-mechanical coupling between ATP hydrolysis and DNA translocation. Instead, significantly less is known about the small terminase subunit, TerS, which is dispensable or even inhibitory in vitro, but essential in vivo. By taking advantage of the recent revolution in cryo-electron microscopy (cryo-EM) and building upon a …
Breaking Symmetry In Viral Icosahedral Capsids As Seen Through The Lenses Of X-Ray Crystallography And Cryo-Electron Microscopy., Kristin N. Parent, Jason R. Schrad, Gino Cingolani
Breaking Symmetry In Viral Icosahedral Capsids As Seen Through The Lenses Of X-Ray Crystallography And Cryo-Electron Microscopy., Kristin N. Parent, Jason R. Schrad, Gino Cingolani
Department of Biochemistry and Molecular Biology Faculty Papers
The majority of viruses on Earth form capsids built by multiple copies of one or more types of a coat protein arranged with 532 symmetry, generating an icosahedral shell. This highly repetitive structure is ideal to closely pack identical protein subunits and to enclose the nucleic acid genomes. However, the icosahedral capsid is not merely a passive cage but undergoes dynamic events to promote packaging, maturation and the transfer of the viral genome into the host. These essential processes are often mediated by proteinaceous complexes that interrupt the shell's icosahedral symmetry, providing a gateway through the capsid. In this review, …