Chlamydiaphage Chp2, a skeleton in the ?X174 closet: scaffolding protein and procapsid identification
Chlamydiaphage Chp2, a skeleton in the ?X174 closet: scaffolding protein and procapsid identification
Chlamydiaphage Chp2 is a member of the family Microviridae, of which bacteriophage X174 is the type species. Although grouped in the same family, the relationship between the Microviridae coliphages and the Chp2-like viruses, which infect obligate intracellular parasitic bacteria, is quite distant, with major differences in structural protein content and scaffolding protein dependence. To investigate the morphogenesis of Chp2, large particles were isolated from infected Chlamydophila abortus by equilibrium and rate zonal sedimentation.
A monoclonal antibody that recognizes only assembled viral coat proteins was used in these detection assays. Thus, the detected particles represent virions and/or postcapsid formation assembly intermediates. Two distinct particle types were detected, differing in both protein and DNA content. Filled particles lacked VP3, the putative internal scaffolding protein, whereas empty particles contained this protein. These results indicate that VP3 is a scaffolding protein and that the isolated VP3-containing particles most likely represent Chp2 procapsids.
7571-7574
Clarke, Ian N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b
Cutcliffe, Leslie T.
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Everson, J. Sylvia
4f48e7a8-2e65-44fe-900f-d55d5d32a4a8
Garner, Sarah A.
0965edba-1d1f-4080-85a0-41b53d3cb553
Lambden, Paul R.
4fcd536e-2d9a-4366-97c6-386e6b005698
Pead, Paddy J.
06abdd20-52a4-478e-b1bc-3df8fe7eb85e
Pickett, Mark A.
4b358cb6-2f2e-4691-a314-0e80df48eadb
Brentlinger, Karie L.
32364402-d17b-43cc-a36a-3e5c94639c0f
Fane, Bentley A.
18eefa7a-5999-4e03-8ebb-f16e05e3af13
2004
Clarke, Ian N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b
Cutcliffe, Leslie T.
64b28f0c-6519-4ec2-907d-812f3f3b4049
Everson, J. Sylvia
4f48e7a8-2e65-44fe-900f-d55d5d32a4a8
Garner, Sarah A.
0965edba-1d1f-4080-85a0-41b53d3cb553
Lambden, Paul R.
4fcd536e-2d9a-4366-97c6-386e6b005698
Pead, Paddy J.
06abdd20-52a4-478e-b1bc-3df8fe7eb85e
Pickett, Mark A.
4b358cb6-2f2e-4691-a314-0e80df48eadb
Brentlinger, Karie L.
32364402-d17b-43cc-a36a-3e5c94639c0f
Fane, Bentley A.
18eefa7a-5999-4e03-8ebb-f16e05e3af13
Clarke, Ian N., Cutcliffe, Leslie T., Everson, J. Sylvia, Garner, Sarah A., Lambden, Paul R., Pead, Paddy J., Pickett, Mark A., Brentlinger, Karie L. and Fane, Bentley A.
(2004)
Chlamydiaphage Chp2, a skeleton in the ?X174 closet: scaffolding protein and procapsid identification.
Journal of Bacteriology, 186 (22), .
(doi:10.1128/JB.186.22.7571-7574.2004).
Abstract
Chlamydiaphage Chp2 is a member of the family Microviridae, of which bacteriophage X174 is the type species. Although grouped in the same family, the relationship between the Microviridae coliphages and the Chp2-like viruses, which infect obligate intracellular parasitic bacteria, is quite distant, with major differences in structural protein content and scaffolding protein dependence. To investigate the morphogenesis of Chp2, large particles were isolated from infected Chlamydophila abortus by equilibrium and rate zonal sedimentation.
A monoclonal antibody that recognizes only assembled viral coat proteins was used in these detection assays. Thus, the detected particles represent virions and/or postcapsid formation assembly intermediates. Two distinct particle types were detected, differing in both protein and DNA content. Filled particles lacked VP3, the putative internal scaffolding protein, whereas empty particles contained this protein. These results indicate that VP3 is a scaffolding protein and that the isolated VP3-containing particles most likely represent Chp2 procapsids.
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Published date: 2004
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Local EPrints ID: 26991
URI: http://eprints.soton.ac.uk/id/eprint/26991
ISSN: 0021-9193
PURE UUID: 179dec45-f5a6-4c64-b86c-1119c07c3b0f
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Date deposited: 27 Apr 2006
Last modified: 16 Mar 2024 02:33
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Author:
Leslie T. Cutcliffe
Author:
J. Sylvia Everson
Author:
Sarah A. Garner
Author:
Paul R. Lambden
Author:
Paddy J. Pead
Author:
Mark A. Pickett
Author:
Karie L. Brentlinger
Author:
Bentley A. Fane
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