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Structural changes of tailless bacteriophage ΦX174 during penetration of bacterial cell walls.
Sun, Yingyuan; Roznowski, Aaron P; Tokuda, Joshua M; Klose, Thomas; Mauney, Alexander; Pollack, Lois; Fane, Bentley A; Rossmann, Michael G.
Afiliação
  • Sun Y; Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.
  • Roznowski AP; The BIO5 Institute, University of Arizona, Tucson, AZ 85721.
  • Tokuda JM; School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853.
  • Klose T; Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.
  • Mauney A; School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853.
  • Pollack L; School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853.
  • Fane BA; The BIO5 Institute, University of Arizona, Tucson, AZ 85721.
  • Rossmann MG; Department of Biological Sciences, Purdue University, West Lafayette, IN 47907; mr@purdue.edu.
Proc Natl Acad Sci U S A ; 114(52): 13708-13713, 2017 12 26.
Article em En | MEDLINE | ID: mdl-29229840
Unlike tailed bacteriophages, which use a preformed tail for transporting their genomes into a host bacterium, the ssDNA bacteriophage ΦX174 is tailless. Using cryo-electron microscopy and time-resolved small-angle X-ray scattering, we show that lipopolysaccharides (LPS) form bilayers that interact with ΦX174 at an icosahedral fivefold vertex and induce single-stranded (ss) DNA genome ejection. The structures of ΦX174 complexed with LPS have been determined for the pre- and post-ssDNA ejection states. The ejection is initiated by the loss of the G protein spike that encounters the LPS, followed by conformational changes of two polypeptide loops on the major capsid F proteins. One of these loops mediates viral attachment, and the other participates in making the fivefold channel at the vertex contacting the LPS.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Parede Celular / Bacteriófago phi X 174 / Proteínas do Capsídeo / Escherichia coli / Internalização do Vírus Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Parede Celular / Bacteriófago phi X 174 / Proteínas do Capsídeo / Escherichia coli / Internalização do Vírus Idioma: En Ano de publicação: 2017 Tipo de documento: Article