The formation of empty shells upon pressure induced decapsidation of turnip yellow mosaic virus

被引:0
作者
M. Leimkühler
A. Goldbeck
M. D. Lechner
M. Adrian
B. Michels
J. Witz
机构
[1]  Physikalische Chemie,
[2] Institut für Chemie,undefined
[3] Universität,undefined
[4] Osnabrück,undefined
[5] Germany,undefined
[6]  Laboratoire d’Analyses Ultrastructurales,undefined
[7] Universitéde Lausanne,undefined
[8] Lausanne,undefined
[9] Switzerland,undefined
[10]  Laboratoire de Dynamique des Fluides Complexes,undefined
[11] UMR 7506 du CNRS,undefined
[12] Université Louis Pasteur,undefined
[13] Strasbourg,undefined
[14] France,undefined
[15]  Immunochimie des Peptides et des Virus,undefined
[16] UPR 9021 du CNRS,undefined
[17] Institut de Biologie Moléculaire et Cellulaire,undefined
[18] Strasbourg,undefined
[19] France,undefined
来源
Archives of Virology | 2001年 / 146卷
关键词
Hydrogen; Electron Microscopy; Hydrogen Bond; High Pressure; Small Angle;
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摘要
 The stability of turnip yellow mosaic virus (TYMV) was investigated under pressure, using solution neutron small angle scattering. Dissociation products were characterized by analytical ultracentrifugation and electron microscopy. At pH 6.0, TYMV remained unaffected by pressure, up to 260 Megapascals (MPa), the highest pressure reached in these experiments. At pH 8.0, TYMV remained unaffected by pressure up to 160 MPa, but decapsidated irreversibly above 200 MPa, giving rise to more and more empty shells upon increasing pressure. The organization of these empty shells was similar to that of the capsid of native virions, apart from the presence of a hole corresponding to the loss of a group of 5–8 coat protein subunits, through which the RNA may have escaped. At variance with other small isometric viruses, the capsid of TYMV never dissociated under pressure into subunits or small aggregates of subunits. This exceptional behavior of TYMV is probably due to the importance of van der Waals contacts and hydrogen bonds in the stability of its capsid.
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页码:653 / 667
页数:14
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