Recent Studies on the Structure of Tobacco Mosaic Virus

Fa, Anderer

doi:10.1016/s0065-3233(08)60267-3

Cited by 53 publications

(5 citation statements)

References 128 publications

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“…TMV protein polymerizes when the concentration and/or temperature is increased and depolymerizes when they are decreased (Lauffer & Stevens, 1968). At a pH of approximately 6.5, TMV CP can be repolymerized into virus-like particles that are structurally similar to native virions (Anderer, 1963;Caspar, 1963;Butler & Klug, 1978;Namba et al, 1989;Butler, 1999). At a pH near 8.0 and at low ionic strength, a mixture of monomers and two-layer trimers, called A-protein, is formed (Schramm & Zillig, 1955;Lauffer & Stevens, 1968;Butler & Klug, 1978;Butler, 1999).…”

mentioning

confidence: 99%

Thermal transition of native tobacco mosaic virus and RNA-free viral proteins into spherical nanoparticles

Atabekov

Nikitin

Arkhipenko

et al. 2010

Journal of General Virology

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Spherical nanoparticles (SNPs) were generated by two-step thermal remodelling of native tobacco mosaic virus (TMV) at 94 6C. Particles of irregular shape and varying size were generated by TMV at 90 6C. They could be converted into SNPs by heating at 94 6C and were considered to be intermediate precursors of SNPs. In addition to SNP monomers (53 nm diameter), generated by individual TMV virions, large SNPs (100-800 nm diameter) were assembled. The size of the SNPs depended on the TMV concentration. The SNPs could be generated by distinct forms of RNA-free TMV coat protein (CP) aggregates and individual CP subunits. A one-step SNP assembly appeared to occur in these cases. These results show that SNPs represent a new type of particle nanoplatform for producing compositions of SNPs with foreign protein molecules bound to their surface.The rod-like particles of tobacco mosaic virus (TMV) of 18 nm diameter and 300 nm modal length consist of 2130 identical 17.5 kDa protein subunits arranged helically into a rigid tube. The viral RNA is intercalated between the protein turns (Zaitlin & Israel, 1975;Butler, 1999;Klug, 1999). TMV can be disassembled into protein subunits with subsequent reassembly (reconstitution) of viral particles in vitro from the nucleic acid and coat protein (CP) (Butler & Klug, 1978;Fraenkel-Conrat & Singer, 1999;Klug, 1999). In the absence of nucleic acid, the viral CP may be assembled into several types of aggregate. It has been established that polymerization of TMV CP is an endothermic, concentration-dependent and reversible process. TMV protein polymerizes when the concentration and/or temperature is increased and depolymerizes when they are decreased (Lauffer & Stevens, 1968). At a pH of approximately 6.5, TMV CP can be repolymerized into virus-like particles that are structurally similar to native virions (Anderer, 1963;Caspar, 1963;Butler & Klug, 1978;Namba et al., 1989;Butler, 1999). At a pH near 8.0 and at low ionic strength, a mixture of monomers and two-layer trimers, called A-protein, is formed (Schramm & Zillig, 1955;Lauffer & Stevens, 1968;Butler & Klug, 1978;Butler, 1999). The predominant aggregate at neutral pH and low ionic strength is a 20S two-layer polar disc made of 34 subunits (Díaz-Avalos & Caspar, 1998). Lauffer & Price (1940) found that heat inactivation of TMV is closely associated with CP denaturation. Hart (1956) used electron microscopy to analyse the morphological changes induced in TMV by heating and reported that heating in the range 80-98 u C for 10 s resulted in a swelling of TMV particles at one or both ends. Eventually, the rods were converted into 'ball-like particles' with the approximate volume of the original rod.Here, we found that the size of the spherical nanoparticles (SNPs) generated by heating TMV did not necessarily correlate with that of the original rod, but varied in a wide range from approximately 50 to 800 nm. The SNPs were not only generated by the native TMV rods, but were also readily produced by different forms of RNA-free TMV CP. The eviden...

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confidence: 99%

Thermal transition of native tobacco mosaic virus and RNA-free viral proteins into spherical nanoparticles

Atabekov

Nikitin

Arkhipenko

et al. 2010

Journal of General Virology

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“…An Arg residue was placed just N-terminus of the ACEI sequence in TLRTB, and the peptides derived from HA and gpl20 in TLHAI, TLHA2 and TLHIV contained Arg or Lys residues. Since TMV particle is known to be resistant to treatment with trypsin [18], it is likely that only the sequences locating on the surface of the virus particles are digested with trypsin. Proteins of virus particles treated with trypsin were examined by Western blot analysis using an anti-TMV antiserum.…”

Section: Purification Of Virus Particlesmentioning

confidence: 99%

Systemic production of foreign peptides on the particle surface of tobacco mosaic virus

Sugiyama¹,

Hamamoto²,

Takemoto³

et al. 1995

FEBS Letters

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“…The two-layer cylindrical substructure, each layer consisting of a ring of 17 molecules of coat protein (CP), is known as a “disk,” and 16 1/3 molecules are present in each turn of the assembled helix. RNA is introduced between the CP turns and follows the helix of protein subunits [13, 14]. Apparently, the front stereochemical surface of terminal CP molecules of the helical TMV particle is not equivalent to inner surfaces of other CP subunits.…”

Section: Introductionmentioning

confidence: 99%

Production of Platinum Atom Nanoclusters at One End of Helical Plant Viruses

Drygin

Кондакова

Atabekov

2013

Advances in Virology

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Platinum atom clusters (Pt nanoparticles, Pt-NPs) were produced selectively at one end of helical plant viruses, tobacco mosaic virus (TMV) and potato virus X (PVX), when platinum coordinate compounds were reduced chemically by borohydrides. Size of the platinum NPs depends on conditions of the electroless deposition of platinum atoms on the virus. Results suggest that the Pt-NPs are bound concurrently to the terminal protein subunits and the 5′ end of encapsidated TMV RNA. Thus, a special structure of tobacco mosaic virus and potato X virus particles with nanoparticles of platinum, which looks like a push-pin with platinum head and virus needle, was obtained. Similar results were obtained with ultrasonically fragmented TMV particles. By contrast, the Pt-NPs fully filled the central axial hole of in vitro assembled RNA-free TMV-like particles. We believe that the results presented here will be valuable in the fundamental understanding of interaction of viral platforms with ionic metals and in a mechanism of nanoparticles formation.

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Recent Studies on the Structure of Tobacco Mosaic Virus

Cited by 53 publications

References 128 publications

Thermal transition of native tobacco mosaic virus and RNA-free viral proteins into spherical nanoparticles

Thermal transition of native tobacco mosaic virus and RNA-free viral proteins into spherical nanoparticles

Systemic production of foreign peptides on the particle surface of tobacco mosaic virus

Production of Platinum Atom Nanoclusters at One End of Helical Plant Viruses

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