Non-Stem Amino Acids Are Involved in the Phage P22 TSP NTD Stability


The P22 phage system is an intensely studied model system. Studies have ranged from biochemical analysis of basic life processes to the use of this phage for phage therapy. The phage tailspike protein (TSP) has itself been the subject of intensive studies over the past fifty years. The P22 TSP is essential for initiation of the infection process and instrumental as the last protein assembled onto the phage particle structure to complete its assembly. It has also been the subject for many structural studies including cryoelectron microscopic analysis and photophysical studies. It has been a model for in vivo and in vitro protein folding including analysis using P22 TSP temperature-sensitive for folding mutations (tsf). Recently the structure and function of the N-terminal domain (NTD), including some aspects of the structural stability of the P22 TSP NTD (aa1-aa108), are being genetically dissected. This report strongly supports the notion that two amino acids, not localized to the internal NTD dome stem, are important in the structural stability of the P22 TSP NTD.

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Venkatesan, K. , Williams, J. and Villafane, R. (2014) Non-Stem Amino Acids Are Involved in the Phage P22 TSP NTD Stability. Advances in Microbiology, 4, 521-526. doi: 10.4236/aim.2014.49058.

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The authors declare no conflicts of interest.


[1] Aksyuk, A.A. and Rossmann, M.G. (2011) Bacteriophage Assembly. Viruses, 3, 172-203.
[2] Casjens, S.R. and Thuman-Commike, P.A. (2011) Evolution of Mosaically Related Tailed Bacteriophage Genomes Seen through the Lens of Phage P22 Virion Assembly. Virology, 411, 393-415.
[3] Strauss, H. and King, J. (1984) Steps in the Stabilization of Newly Packaged DNA during Phage P22 Morphogenesis. Journal of Molecular Biology, 172, 523-543.
[4] Hyrc, C.F., Chen, D.-H. and Chiu, W. (2011) Near-Atomic Resolution Cryo-EM for Molecular Virology. Current Opinion in Virology, 21, 110-117.
[5] Lander, G.C., Khayat, R., Li, R., Prevelige, P.E., Porter, C.S. and Carragher, B. (2009) The P22 Tail Machine at Subnanometer Resolution Reveals the Architecture of an Infectious Conduit. Structure, 17, 789-799.
[6] Ackermann, H. (2009) Phage Classification and Characterization. Methods in Molecular Biology, 501, 127-140.
[7] Israel, V., Anderson, T.F. and Levine, M. (1967) In Vitro Morphogenesis of Phage P22 from Heads and Base-Plate Parts. Proceedings of the National Academy of Sciences, 57, 284-291.
[8] Israel, V. (1978) Role of the Bacteriophage P22 Tail in the Early Stages of Infection. Journal of Virology, 18, 361-364.
[9] Goldenberg, D.P. and King, J. (1982) Trimeric Intermediate in the in Vivo Folding and Subunit Assembly of the Tailspike Endorhamnosidase of Bacteriophage P22. Proceedings of the National Academy of Sciences, 79, 3403-3407.
[10] Sauer, R.T., Krovatin, W., Poteete, A.R. and Berget, P.B. (1982) Phage P22 Tail Protein: Gene and Amino Acid Sequence. Biochemistry, 21, 5811-5815.
[11] Shin, H., Lee, J.-H., Kim, H., Choi, Y., Heu, S. and Ryu, S. (2012) Receptor Diversity and Host Interaction of Bacteriophages Infecting Salmonella enteric SerovarTyphimurium. PLoS ONE, 7, e43392.
[12] Sturtevant, J.M., Yu, M.-H., Haase-Pettingell, C. and King, J. (1989) Thermostability of Temperature-Sensitive Folding Mutants of the P22 Tailspike Protein. The Journal of Biological Chemistry, 264, 10693-10698.
[13] Goldenberg, D.P., Berget, P.B. and King, J. (1982) Maturation of the Tail Spike Endorhamnosidase of Salmonella Phage P22. The Journal of Biological Chemistry, 257, 7864-7871.
[14] Andres, D., Hanke, C., Baxa, U., Seul, A., Barbirz, S. and Seckler, R. (2010) Tailspike Interactions with Lipopolysaccharide Effect: DNA Ejection from the Phage P22 Particles in Vitro. Journal of Biological Chemistry, 285, 36768-36775.
[15] Steinbacher, S., Miller, S., Baxa, U., Budisa, N., Weintraub, A., Seckler, R. and Huber, R. (1997) Phage P22 Tailspike Protein: Crystal Structure of the Head-Binding Domain at 2.3 A, Fully Refined Structure of the Endorhamnosidase at 1.56 A Resolution, and the Molecular Basis of O-Antigen Recognition and Cleavage. Journal of Molecular Biology, 267, 865-880.
[16] Palmer, C., Williams, J., Dean, D., Johnson, S., Wu, H., Robertson, B.K., Jackson, D. and Villafane, R. (2014) Stem Mutants in the N-Terminal Domain of the Phage P22 Tailspike Protein. American Journal of Microbiological Research, 2, 1-7.
[17] Schwarz, J.J. and Berget, P. (1989) The Isolation and Sequence of Missense and Nonsense Mutations in the Cloned Bacteriophage P22 Tailspike Protein Gene. Genetics, 121, 635-649.
[18] Sambrook, J., Fritsch, E. and Maniatis, T. (1989) Molecular Cloning. 2nd Edition, Cold Spring Harbor Laboratory Press, Plainview.
[19] Manning, M. and Colon, W. (2004) Structural Basis of Protein Kinetic Stability: Resistance to Sodium Dodecyl Sulfate Suggests a Central Role for Rigidity and a Bias Toward-Sheet Structure. Biochemistry, 43, 11248-1125.
[20] Maurides, P.A., Schwarz, J.J. and Berget, P.B. (1990) Intragenic Suppression of a Capsid Assembly-Defective P22 Tailspike Mutation. Genetics, 125, 673-681.
[21] Chen, B.-L. and King, J. (1991) Thermal Unfolding Pathway for the Thermostable P22 Tailspike Endorhamnosidase. Biochemistry, 30, 6260-6269.

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