Unique Tail Appendages of Marine Bacteriophages
Affiliation(s)
Department of Molecular Biology and Biochemistry, University of California, Irvine, USA.
Department of Molecular Biology and Biochemistry, University of California, Irvine, USA.
ABSTRACT
The objective was to visualize a variety of marine bacteriophage and identify unique structural features that set them apart from terrestrial phages. Phages were plaque isolated and characterized using atomic force microscopy. Bacteriophage infecting cyanobacteria synechococcus that exhibits a novel structural feature not previously reported for any other phages were observed. These cyanophages have up to four, 450 nm long, multi-stranded, complex helical fibers that emanate from either the base plate and/or the collar of the phage particle, origins of shorter fibers on well-studied phages such as T4. The flexible fibers terminate at their distal ends in multiple bulbs of diameter 30 nm composed of 20 to 30 closely associated proteins. Bulbs form one of two distinctive patterns, or tassels. Most commonly, the arrangement is a 3 + 1 pattern of three consecutive bulbs at the very end with a forth lying upstream, separated from the terminal three by a gap of 135 nm. In other populations the fibers terminate in 5 consecutive bulbs. It is proposed that the novel appendages may be involved in host cell searching and recognition in a marine environment.
The objective was to visualize a variety of marine bacteriophage and identify unique structural features that set them apart from terrestrial phages. Phages were plaque isolated and characterized using atomic force microscopy. Bacteriophage infecting cyanobacteria synechococcus that exhibits a novel structural feature not previously reported for any other phages were observed. These cyanophages have up to four, 450 nm long, multi-stranded, complex helical fibers that emanate from either the base plate and/or the collar of the phage particle, origins of shorter fibers on well-studied phages such as T4. The flexible fibers terminate at their distal ends in multiple bulbs of diameter 30 nm composed of 20 to 30 closely associated proteins. Bulbs form one of two distinctive patterns, or tassels. Most commonly, the arrangement is a 3 + 1 pattern of three consecutive bulbs at the very end with a forth lying upstream, separated from the terminal three by a gap of 135 nm. In other populations the fibers terminate in 5 consecutive bulbs. It is proposed that the novel appendages may be involved in host cell searching and recognition in a marine environment.
Cite this paper
Y. Kuznetsov, S. Chang, A. Credaroli and A. McPherson, "Unique Tail Appendages of Marine Bacteriophages," Advances in Microbiology, Vol. 3 No. 6, 2013, pp. 55-59. doi: 10.4236/aim.2013.36A007.
Y. Kuznetsov, S. Chang, A. Credaroli and A. McPherson, "Unique Tail Appendages of Marine Bacteriophages," Advances in Microbiology, Vol. 3 No. 6, 2013, pp. 55-59. doi: 10.4236/aim.2013.36A007.
References
[1] Y. G. Kuznetsov, et al., “Imaging of viruses by atomic force microscopy,” Journal of General Virology, Vol. 82, No. 9, 2001, pp. 2025-2034. [2] A. J. Malkin, M. Plomp and A. McPherson, “Unraveling the Architecture of Viruses by High-Resolution Atomic Force Microscopy,” In: Virus Structure and Imaging, DNA Viruses, Methods and Protocols, Humana Press, Totowa, 2004, pp. 85-108. [3] Y. G. Kuznetsov, J. B. Martiny and A. McPherson, “Structural Analysis of a Synechococcus myovirus S-CAM4 and Infected Cells by Atomic Force Microscopy,” Journal of General Virology, Vol. 91, No. 12, 2010, pp. 3095-104. http://dx.doi.org/10.1099/vir.0.025254-0 [4] Y. G. Kuznetsov and A. McPherson, “Atomic Force Microscopy (AFM) in the Imaging of Viruses and Virus Infected Cells,” Microbiology and Molecular Biology Reviews (MMBR), Vol. 75, No. 2, 2011, pp. 268-285.
http://dx.doi.org/10.1128/MMBR.00041-10 [5] H. G. Hansma and J. H. Hoh, “Biomolecular imaging with the atomic force microscope,” Annual Review of Biophysics and Biomolecular Structure, Vol. 23, 1994, pp. 115-139.
http://dx.doi.org/10.1146/annurev.bb.23.060194.000555 [6] H. G. Hansma and L. Pietrasanta, “Atomic Force Microscopy and Other Scanning Probe Microscopies,” Current Opinion in Chemical Biology, Vol. 2, No. 5, 1998, pp. 579-584. http://dx.doi.org/10.1016/S1367-5931(98)80086-0 [7] E. Kutter and A. Sulakvelidze, “Bacteriophages: Biology and Applications,” CRC Press, Boca Raton, 2004.
http://dx.doi.org/10.1016/S1367-5931(98)80086-0 [8] F. A. Eiserling, “Structure of the T4 Virion. in Bacteriophage T4,” American Society for Microbiology, Washington, D.C., 1983. [9] C. K. Matthews, et al., “Bacteriophage T4,” Microbiol Press, Washington, D.C., 1983. [10] W. B. Wood and R. A. Crowther, “Long Tail Fibers: Genes, Proteins, Assembly and Structure,” In: C. K. Mathews, et al., Eds., Bacteriophage T4, American Society for Microbiology, Washington, D.C., 1983. [11] E. Moutevelis and D. N. Woolfson, “A Periodic Table of Coiled-Coil Protein Structures,” Journal of Molecular Biology, Vol. 385, No. 3, 2009, pp. 726-732.
http://dx.doi.org/10.1016/j.jmb.2008.11.028 [12] D. N. Woolfson, “The Design of Coiled-Coil Structures and Assemblies,” Advances in Protein Chemistry, Vol. 70, 2005, pp. 79-112.
http://dx.doi.org/10.1016/S0065-3233(05)70004-8
[1] Y. G. Kuznetsov, et al., “Imaging of viruses by atomic force microscopy,” Journal of General Virology, Vol. 82, No. 9, 2001, pp. 2025-2034. [2] A. J. Malkin, M. Plomp and A. McPherson, “Unraveling the Architecture of Viruses by High-Resolution Atomic Force Microscopy,” In: Virus Structure and Imaging, DNA Viruses, Methods and Protocols, Humana Press, Totowa, 2004, pp. 85-108. [3] Y. G. Kuznetsov, J. B. Martiny and A. McPherson, “Structural Analysis of a Synechococcus myovirus S-CAM4 and Infected Cells by Atomic Force Microscopy,” Journal of General Virology, Vol. 91, No. 12, 2010, pp. 3095-104. http://dx.doi.org/10.1099/vir.0.025254-0 [4] Y. G. Kuznetsov and A. McPherson, “Atomic Force Microscopy (AFM) in the Imaging of Viruses and Virus Infected Cells,” Microbiology and Molecular Biology Reviews (MMBR), Vol. 75, No. 2, 2011, pp. 268-285.
http://dx.doi.org/10.1128/MMBR.00041-10 [5] H. G. Hansma and J. H. Hoh, “Biomolecular imaging with the atomic force microscope,” Annual Review of Biophysics and Biomolecular Structure, Vol. 23, 1994, pp. 115-139.
http://dx.doi.org/10.1146/annurev.bb.23.060194.000555 [6] H. G. Hansma and L. Pietrasanta, “Atomic Force Microscopy and Other Scanning Probe Microscopies,” Current Opinion in Chemical Biology, Vol. 2, No. 5, 1998, pp. 579-584. http://dx.doi.org/10.1016/S1367-5931(98)80086-0 [7] E. Kutter and A. Sulakvelidze, “Bacteriophages: Biology and Applications,” CRC Press, Boca Raton, 2004.
http://dx.doi.org/10.1016/S1367-5931(98)80086-0 [8] F. A. Eiserling, “Structure of the T4 Virion. in Bacteriophage T4,” American Society for Microbiology, Washington, D.C., 1983. [9] C. K. Matthews, et al., “Bacteriophage T4,” Microbiol Press, Washington, D.C., 1983. [10] W. B. Wood and R. A. Crowther, “Long Tail Fibers: Genes, Proteins, Assembly and Structure,” In: C. K. Mathews, et al., Eds., Bacteriophage T4, American Society for Microbiology, Washington, D.C., 1983. [11] E. Moutevelis and D. N. Woolfson, “A Periodic Table of Coiled-Coil Protein Structures,” Journal of Molecular Biology, Vol. 385, No. 3, 2009, pp. 726-732.
http://dx.doi.org/10.1016/j.jmb.2008.11.028 [12] D. N. Woolfson, “The Design of Coiled-Coil Structures and Assemblies,” Advances in Protein Chemistry, Vol. 70, 2005, pp. 79-112.
http://dx.doi.org/10.1016/S0065-3233(05)70004-8