Zobrazeno 1 - 10
of 86
pro vyhledávání: '"Carolyn M. Teschke"'
Autor:
Justin C. Leavitt, Brianna M. Woodbury, Eddie B. Gilcrease, Charles M. Bridges, Carolyn M. Teschke, Sherwood R. Casjens
Publikováno v:
mBio, Vol 15, Iss 2 (2024)
ABSTRACT Many temperate phages encode prophage-expressed functions that interfere with superinfection of the host bacterium by external phages. Salmonella phage P22 has four such systems that are expressed from the prophage in a lysogen that are enco
Externí odkaz:
https://doaj.org/article/4121e668a2364066b13c961ebd45b005
Autor:
Brianna M. Woodbury, Tina Motwani, Makayla N. Leroux, Lauren F. Barnes, Nicholas A. Lyktey, Sanchari Banerjee, Corynne L. Dedeo, Martin F. Jarrold, Carolyn M. Teschke
Publikováno v:
Viruses, Vol 14, Iss 7, p 1400 (2022)
The oligomerization and incorporation of the bacteriophage P22 portal protein complex into procapsids (PCs) depends upon an interaction with scaffolding protein, but the region of the portal protein that interacts with scaffolding protein has not bee
Externí odkaz:
https://doaj.org/article/e9045634e7dd4872a8e106b9a7a8c50f
Autor:
Justin C. Leavitt, Eddie B. Gilcrease, Brianna M. Woodbury, Carolyn M. Teschke, Sherwood R. Casjens
Publikováno v:
Viruses, Vol 13, Iss 8, p 1504 (2021)
Tailed double-stranded DNA bacteriophages inject some proteins with their dsDNA during infection. Phage P22 injects about 12, 12, and 30 molecules of the proteins encoded by genes 7, 16 and 20, respectively. After their ejection from the virion, they
Externí odkaz:
https://doaj.org/article/3f9423c17313483f87404d98ba7e49b0
Autor:
Ravi K. Lokareddy, Rajeshwer S. Sankhala, Ankoor Roy, Pavel V. Afonine, Tina Motwani, Carolyn M. Teschke, Kristin N. Parent, Gino Cingolani
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
Tailed bacteriophages assemble empty precursor capsids known as procapsids that are subsequently filled with viral DNA by a genome-packaging motor. Here the authors present a structure-based analysis that suggests the signal for termination of genome
Externí odkaz:
https://doaj.org/article/9153c6cc3a8e422c89bc78e6f3ac607c
Publikováno v:
Viruses, Vol 12, Iss 10, p 1163 (2020)
Decoration proteins are viral accessory gene products that adorn the surfaces of some phages and viral capsids, particularly tailed dsDNA phages. These proteins often play a “cementing” role, reinforcing capsids against accumulating internal pres
Externí odkaz:
https://doaj.org/article/7d7a2bfe8e574a3f9d17233909fd9ec6
Autor:
Weimin Wu, Justin C. Leavitt, Naiqian Cheng, Eddie B. Gilcrease, Tina Motwani, Carolyn M. Teschke, Sherwood R. Casjens, Alasdair C. Steven
Publikováno v:
mBio, Vol 7, Iss 4 (2016)
ABSTRACT The P22 capsid is a T=7 icosahedrally symmetric protein shell with a portal protein dodecamer at one 5-fold vertex. Extending outwards from that vertex is a short tail, and putatively extending inwards is a 15-nm-long α-helical barrel forme
Externí odkaz:
https://doaj.org/article/9b9b267307a1486f8926e69d4dbbe79f
Autor:
Rebecca L Newcomer, Jason R Schrad, Eddie B Gilcrease, Sherwood R Casjens, Michael Feig, Carolyn M Teschke, Andrei T Alexandrescu, Kristin N Parent
Publikováno v:
eLife, Vol 8 (2019)
The major coat proteins of dsDNA tailed phages (order Caudovirales) and herpesviruses form capsids by a mechanism that includes active packaging of the dsDNA genome into a precursor procapsid, followed by expansion and stabilization of the capsid. Th
Externí odkaz:
https://doaj.org/article/a94a86477c72462ea6b6085239e80eb8
Publikováno v:
Journal of Biomolecular NMR.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::73d53b9aea84e246d784e5d3ff345359
https://doi.org/10.1007/s10858-023-00414-7
https://doi.org/10.1007/s10858-023-00414-7
Scaffolding proteins are essential for the assembly of most tailed, double-stranded DNA bacteriophages as well as herpesviruses. These proteins interact specifically with the coat proteins to efficiently assemble procapsids with the correct morpholog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cb2111005303cee1f01aa298cc9168af
https://doi.org/10.1101/2022.12.13.520362
https://doi.org/10.1101/2022.12.13.520362
Autor:
Fenglin Li, Chun-Feng David Hou, Ruoyu Yang, Richard Whitehead, Carolyn M. Teschke, Gino Cingolani
Publikováno v:
Science Advances. 8
Sf6 is a bacterial virus that infects the human pathogen Shigella flexneri. Here, we describe the cryo–electron microscopy structure of the Sf6 tail machine before DNA ejection, which we determined at a 2.7-angstrom resolution. We built de novo str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb36553b89ff82a254ae247d1760e036
https://doi.org/10.1126/sciadv.adc9641
https://doi.org/10.1126/sciadv.adc9641