The stability of belladonna mottle virus (BDMV) has been studied with respect to elevated pH and to freezing and thawing. BDMV, purified by a modified procedure, was stable at alkaline pH, in contradiction to earlier reports. This difference in the stability could be attributed to the presence of 90 to 140 molecules of spermidine, 20 to 50 molecules of putrescine and 500 to 900 calcium ions in each virus particle. The polyamines could be easily exchanged with other cations such as potassium or caesium and this resulted in a loss of particle stability. These cations may therefore play a role in maintaining the integrity of particle structure. The formation of empty protein shells as a result of freezing and thawing BDMV particles parallels earlier observations on turnip yellow mosaic virus particles.

Keyword(s): BDMV , capsid stability and polyamines

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