Bacteriophage P22 tail accessory factor GP26 is a long triple-stranded coiled-coil

Dewan Andrews, James S. Butler, Jawdat Al-Bassam, Lisa Joss, Danella A. Winn-Stapley, Sherwood Casjens, Gino Cingolani

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

P22 is a well characterized tailed bacteriophage that infects Salmonella enterica serovar Typhimurium. It is characterized by a "short" tail, which is formed by five proteins: the dodecameric portal protein (gp1), three tail accessory factors (gp4, gp10, gp26), and six trimeric copies of the tail-spike protein (gp9). We have isolated the gene encoding tail accessory factor gp26, which is responsible for stabilization of viral DNA within the mature phage, and using a variety of biochemical and biophysical techniques we show that gp26 is very likely a triple stranded coiled-coil protein. Electron microscopic examination of purified gp26 indicates that the protein adopts a rod-like structure ∼210 Å in length. This trimeric rod displays an exceedingly high intrinsic thermostability (Tm ∼85°C), which suggests a potentially important structural role within the phage tail apparatus. We propose that gp26 forms the thin needle-like fiber emanating from the base of the P22 neck that has been observed by electron microscopy of negatively stained P22 virions. By analogy with viral trimeric coiled-coil class I membrane fusion proteins, gp26 may represent the membrane-penetrating device used by the phage to pierce the host outer membrane.

Original languageEnglish (US)
Pages (from-to)5929-5933
Number of pages5
JournalJournal of Biological Chemistry
Volume280
Issue number7
DOIs
StatePublished - Feb 18 2005
Externally publishedYes

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Bacteriophage P22
Bacteriophages
Accessories
Proteins
Membrane Fusion Proteins
Membranes
Salmonella
Gene encoding
Salmonella enterica
Viral DNA
Virion
Needles
Electron microscopy
Electron Microscopy
Microscopic examination
Neck
Stabilization
Electrons
Equipment and Supplies
Fibers

ASJC Scopus subject areas

  • Biochemistry

Cite this

Andrews, D., Butler, J. S., Al-Bassam, J., Joss, L., Winn-Stapley, D. A., Casjens, S., & Cingolani, G. (2005). Bacteriophage P22 tail accessory factor GP26 is a long triple-stranded coiled-coil. Journal of Biological Chemistry, 280(7), 5929-5933. https://doi.org/10.1074/jbc.C400513200

Bacteriophage P22 tail accessory factor GP26 is a long triple-stranded coiled-coil. / Andrews, Dewan; Butler, James S.; Al-Bassam, Jawdat; Joss, Lisa; Winn-Stapley, Danella A.; Casjens, Sherwood; Cingolani, Gino.

In: Journal of Biological Chemistry, Vol. 280, No. 7, 18.02.2005, p. 5929-5933.

Research output: Contribution to journalArticle

Andrews, D, Butler, JS, Al-Bassam, J, Joss, L, Winn-Stapley, DA, Casjens, S & Cingolani, G 2005, 'Bacteriophage P22 tail accessory factor GP26 is a long triple-stranded coiled-coil', Journal of Biological Chemistry, vol. 280, no. 7, pp. 5929-5933. https://doi.org/10.1074/jbc.C400513200
Andrews D, Butler JS, Al-Bassam J, Joss L, Winn-Stapley DA, Casjens S et al. Bacteriophage P22 tail accessory factor GP26 is a long triple-stranded coiled-coil. Journal of Biological Chemistry. 2005 Feb 18;280(7):5929-5933. https://doi.org/10.1074/jbc.C400513200
Andrews, Dewan ; Butler, James S. ; Al-Bassam, Jawdat ; Joss, Lisa ; Winn-Stapley, Danella A. ; Casjens, Sherwood ; Cingolani, Gino. / Bacteriophage P22 tail accessory factor GP26 is a long triple-stranded coiled-coil. In: Journal of Biological Chemistry. 2005 ; Vol. 280, No. 7. pp. 5929-5933.
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