Titration behaviour of three strains of tobacco mosaic virus.
Hydrogen ion titration curves of the virions and proteins of three strains of tobacco mosaic virus (Y-TAMV, U2, and cowpea) were measured in the absence and the presence of Ca2+, Mg2+, or Mn2+ ions, and compared with the analogous curves for the type strain (vulgare). Extinction coefficients were also measured for all four strains' virions and proteins. Y-TAMV is very like vulgare in its cation affinities: the virion has probably three groups per protein subunit that titrate near neutral pH and significantly bind metal ions; the RNA-free protein has very little affinity for Ca2+, although moderate Ca2+ concentrations favour the existence of larger polymers. U2 and cowpea strain virions bind cations significantly more strongly than do Y-TAMV or vulgare virions: their polymerized proteins, too, have significant affinities for Ca2+ ions, which make their titration and sedimentation behaviours relatively sensitive to added calcium. These cation-binding differences correspond well with the differences between the strains' protein sequences. The features common to all four strains are that the virions are apparently structurally invariant and have at least one site per subunit with Ca2+ affinity in the region of 10(-5)M, while the RNA-free proteins lack the high-affinity sites but have weaker Ca2+ affinities in the region of 10(-3)M. Some of the cation-binding sites probably lie near the central holes of the virions.
Hendry
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Department of Microbiology, Rhodes University, Grahamstown 6140, South Africa.
Durham
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