Structures of plant viruses from vibrational circular dichroism.
Vibrational circular dichroism (VCD) spectra in the amide I and II regions have been measured for viruses for the first time. VCD spectra were recorded for films prepared from aqueous buffer solutions and also for solutions using D(2)O buffers at pH 8. Investigations of four filamentous plant viruses, Tobacco mosaic virus (TMV), Papaya mosaic virus, Narcissus mosaic virus (NMV) and Potato virus X (PVX), as well as a deletion mutant of PVX, are described in this paper. The film VCD spectra of the viruses clearly revealed helical structures in the virus coat proteins; the nucleic acid bases present in the single-stranded RNA could also be characterized. In contrast, the solution VCD spectra showed the characteristic VCD bands for alpha-helical structures in the coat proteins but not for RNA. Both sets of results clearly indicated that the coat protein conformations are dominated by helical structures, in agreement with earlier reports. VCD results also indicated that the coat protein structures in PVX and NMV are similar to each other and somewhat different from that of TMV. The present study demonstrates the feasibility of measuring VCD spectra for viruses and extracting structural information from these spectra.
Shanmugam
Ganesh
G
Department of Chemistry, Vanderbilt University, Nashville, TN 37235, USA.
Polavarapu
Prasad L
PL
Department of Chemistry, Vanderbilt University, Nashville, TN 37235, USA.
Kendall
Amy
A
Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235, USA.
Stubbs
Gerald
G
Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235, USA.
D036022:Capsid Proteins / Q000032:analysis / Q000737:chemistry; D002942:Circular Dichroism; D010942:Plant Viruses / Q000737:chemistry*; D017433:Protein Structure, Secondary
D036022:Capsid Proteins