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Gene Review

gp32  -  capsid protein

Pseudomonas phage phiKMV

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Disease relevance of gp32

  • A tail-deletion mutant was found to present two preferred views of phage heads: views along the axis through the capsid vertex where the connector protein resides and via which DNA is packaged; and side views perpendicular to this axis [1].
  • Processing determinants required for in vitro cleavage of the poliovirus P1 precursor to capsid proteins [2].
  • The capsid precursor protein (Gag) of Mason-Pfizer monkey virus, the prototype type D retrovirus, has been expressed to high levels in bacteria under the control of the phage T7 promoter [3].
  • Studies using monoclonal antibodies specific for conformational epitopes indicated that the antigenicity of the synthetic particles was similar to whole virions and natural empty capsid particles [4].
  • Intracellular expression and processing of foot-and-mouth disease virus capsid precursors using vaccinia virus vectors: influence of the L protease [5].

High impact information on gp32

  • The first structure reveals a complex assembly in the interior of the capsid, which involves the scaffolding, and the core complex, which plays an important role in DNA packaging and is located in one of the phage vertices [6].
  • We show here that active T4 replication forks, which catalyze the coordinated synthesis of leading and lagging strands, remain stable in the face of dilution provided that the gp44/62 clamp loader, the gp45 sliding clamp, and the gp32 ssDNA-binding protein are present at sufficient levels after dilution [7].
  • Phage virions containing a mutant gp16, a protein known to be ejected from the phage capsid into the cell at the initiation of infection, allow complete entry of the T7 genome in the absence of transcription [8].
  • This process exhibits pseudo-zero-order reaction kinetics and a temperature dependence of translocation rate that are not expected if DNA ejection from a phage capsid were caused by a physical process [9].
  • We have combined a novel technique based on the display of cDNA libraries on the capsid of bacteriophage lambda and an efficient plaque assay to reveal phage displaying ligands that are enriched after only a couple of affinity purification steps [10].

Chemical compound and disease context of gp32

  • Electron microscopy revealed an isometric capsid with dimensions of 54 nm between opposite apices, and a short, noncontractile tail 16 nm long, placing phage WPK into morphogroup C1 [11].

Biological context of gp32


Anatomical context of gp32


Associations of gp32 with chemical compounds

  • The purified proteins reacted in the presence of polyethylene glycol or dextran to produce prohead-like capsid shells and also polycapsids consisting primarily of head protein, similar to the polycapsids observed after infection by T7 mutants lacking connector or core proteins [17].
  • The inclusion bodies and enclosed capsid-like structures were solubilized completely in 8 M urea, but following renaturation, we observed assembly in vitro of capsid-like structures that demonstrated apparent icosahedral symmetry [3].
  • Analysis by sucrose gradient centrifugation showed that material which co-sedimented with natural empty capsid particles (70S) was formed [4].

Other interactions of gp32

  • Production of the major processed capsid protein, gp23, was reduced significantly more than that of most other T4 proteins in unadapted cells relative to adapted cells [18].

Analytical, diagnostic and therapeutic context of gp32


  1. Encapsidated conformation of bacteriophage T7 DNA. Cerritelli, M.E., Cheng, N., Rosenberg, A.H., McPherson, C.E., Booy, F.P., Steven, A.C. Cell (1997) [Pubmed]
  2. Processing determinants required for in vitro cleavage of the poliovirus P1 precursor to capsid proteins. Ypma-Wong, M.F., Semler, B.L. J. Virol. (1987) [Pubmed]
  3. Efficient in vivo and in vitro assembly of retroviral capsids from Gag precursor proteins expressed in bacteria. Klikova, M., Rhee, S.S., Hunter, E., Ruml, T. J. Virol. (1995) [Pubmed]
  4. Assembly of foot-and-mouth disease virus empty capsids synthesized by a vaccinia virus expression system. Abrams, C.C., King, A.M., Belsham, G.J. J. Gen. Virol. (1995) [Pubmed]
  5. Intracellular expression and processing of foot-and-mouth disease virus capsid precursors using vaccinia virus vectors: influence of the L protease. Belsham, G.J., Brangwyn, J.K., Ryan, M.D., Abrams, C.C., King, A.M. Virology (1990) [Pubmed]
  6. Maturation of phage T7 involves structural modification of both shell and inner core components. Agirrezabala, X., Martín-Benito, J., Castón, J.R., Miranda, R., Valpuesta, J.M., Carrascosa, J.L. EMBO J. (2005) [Pubmed]
  7. Conditional coupling of leading-strand and lagging-strand DNA synthesis at bacteriophage T4 replication forks. Kadyrov, F.A., Drake, J.W. J. Biol. Chem. (2001) [Pubmed]
  8. Bacteriophage T7 DNA ejection into cells is initiated by an enzyme-like mechanism. Kemp, P., Gupta, M., Molineux, I.J. Mol. Microbiol. (2004) [Pubmed]
  9. No syringes please, ejection of phage T7 DNA from the virion is enzyme driven. Molineux, I.J. Mol. Microbiol. (2001) [Pubmed]
  10. Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1. Zucconi, A., Dente, L., Santonico, E., Castagnoli, L., Cesareni, G. J. Mol. Biol. (2001) [Pubmed]
  11. Partial characterization of coliphage WPK and a comparison with coliphage T3. Loeffelholz, L., Maier, S. Microbiol. Immunol. (1992) [Pubmed]
  12. Expression and identification of hepatitis C virus polyprotein cleavage products. Grakoui, A., Wychowski, C., Lin, C., Feinstone, S.M., Rice, C.M. J. Virol. (1993) [Pubmed]
  13. Construction and characterization of poliovirus subgenomic replicons. Kaplan, G., Racaniello, V.R. J. Virol. (1988) [Pubmed]
  14. The complete genome structure and synthesis of infectious RNA from clones of tomato bushy stunt virus. Hearne, P.Q., Knorr, D.A., Hillman, B.I., Morris, T.J. Virology (1990) [Pubmed]
  15. Protection from proteolysis using a T4::T7-RNAP phage expression-packaging-processing system. Hong, Y.R., Mullaney, J.M., Black, L.W. Gene (1995) [Pubmed]
  16. Direct production and purification of T7 phage display cloned proteins selected and analyzed on microarrays. Nowak, J.E., Chatterjee, M., Mohapatra, S., Dryden, S.C., Tainsky, M.A. BioTechniques (2006) [Pubmed]
  17. Assembly of T7 capsids from independently expressed and purified head protein and scaffolding protein. Cerritelli, M.E., Studier, F.W. J. Mol. Biol. (1996) [Pubmed]
  18. Induction of the heat shock regulon of Escherichia coli markedly increases production of bacterial viruses at high temperatures. Wiberg, J.S., Mowrey-McKee, M.F., Stevens, E.J. J. Virol. (1988) [Pubmed]
  19. Polymorphism of bacteriophage T7. Gabashvili, I.S., Khan, S.A., Hayes, S.J., Serwer, P. J. Mol. Biol. (1997) [Pubmed]
  20. A novel fluorescent probe: europium complex hybridized T7 phage. Liu, C.M., Jin, Q., Sutton, A., Chen, L. Bioconjug. Chem. (2005) [Pubmed]
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