Structure of simian virus 40 II. Symmetry and components of the virus particle

Anderer, F. A.; Schlumberger, H. D.; Koch, Meinrad A.; Hensel, Frank; Eggers, Hans J.

doi:10.1016/0042-6822(67)90303-0

Cited by 108 publications

(52 citation statements)

References 12 publications

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“…They also appear on the 3-fold axes where they are bounded by d and e subunits. a, Adolph et al (1979); b, Anderer et al (1967); c, Baker et al (1983); d, Baker et al (1988Baker et al ( , 1989); e, Baker et al (1991); f, Belnap et al (1993), Baker (1992); g, Caspar (1966); h, Crowther & Amos (1972); i, Crowther et al (1970a);j, Finch (1974); k, ; l, Griffith et al (1992); m, Hagensee et al (1994); n, Kiselev & Klug (1969); o, Klug (1965); p, ; q, Klug & Finch (1968); r, Liddington et al (1991); s, Rayment et al (1982); t, Salunke et al (1986);u, Stehle et al (1994); v, this study; w, Yabe et al (1979). are averages for each set of particle images and were computed over the full particle radius.…”

Section: Sequence Analysismentioning

confidence: 99%

“…The projected image of each tilted model was correlated against the image of each tilted particle. SV40, whose atomic structure and T = 7d symmetry are known (Anderer et al, 1967;Liddington et al, 1991), served as a standard in establishing a self-consistent set of conventions for defining the tilt direction and angle in the EM420 microscope. As an additional control, each reconstruction was rotated by the untilted Θ,Φ,Ω orientation angles and projected.…”

Section: Hand Determinationsmentioning

confidence: 99%

“…Comparisons of model data with "background" image data (carbon film and vitreous water) and with images of the untilted specimen serve as control measurements. SV40, known to be T = 7d (Anderer et al, 1967;Liddington et al, 1991), served as a control to establish a consistent set of conventions for the hand determination experiments. Differences between these data and those listed in Table 2 (i.e.…”

Section: Tablementioning

confidence: 99%

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Conserved Features in Papillomavirus and Polyomavirus Capsids

Belnap

Olson

Cladel

et al. 1996

Journal of Molecular Biology

108

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Capsids of papilloma and polyoma viruses (papovavirus family) are composed of 72 pentameric capsomeres arranged on a skewed icosahedral lattice (triangulation number of seven, T = 7). Cottontail rabbit papillo mavirus (CRPV) was reported previously to be a T = 7laevo (left-handed) structure, whereas human wart virus, simian virus 40, and murine polyomavirus were shown to be T = 7dextro (right-handed). The CRPV structure determined by cryoelectron microscopy and image reconstruction was similar to previously determined structures of bovine papillomavirus type 1 (BPV-1) and human papillomavirus type 1 (HPV-1). CRPV capsids were observed in closed (compact) and open (swollen) forms. Both forms have star-shaped capsomeres, as do BPV-1 and HPV-1, but the open CRPV capsids are ~2 nm larger in radius. The lattice hands of all papillomaviruses examined in this study were found to be T = 7dextro. In the region of maximum contact, papillomavirus capsomeres interact in a manner similar to that found in polyomaviruses. Although papilloma and polyoma viruses have differences in capsid size (~60 versus ~50 nm), capsomere morphology (11 to 12 nm star-shaped versus 8 nm barrel-shaped), and intercapsomere interactions (slightly different contacts between capsomeres), papovavirus capsids have a conserved, 72-pentamer, T = 7dextro structure. These features are conserved despite significant differences in amino acid sequences of the major capsid proteins. The conserved features may be a consequence of stable contacts that occur within capsomeres and flexible links that form among capsomeres.

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Section: Sequence Analysismentioning

confidence: 99%

Section: Hand Determinationsmentioning

confidence: 99%

Section: Tablementioning

confidence: 99%

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Conserved Features in Papillomavirus and Polyomavirus Capsids

Belnap

Olson

Cladel

et al. 1996

Journal of Molecular Biology

108

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“…We compared projections of 3D reconstructions to images of unstained, frozen-hydrated specimens (cryoTEM images). We used simian virus 40 (SV40), a polyomavirus whose handedness was previously established by electron microscopy (Anderer et al, 1967) and X-ray crystallography (Liddington et al, 1991), as a control in establishing a self-consistent set of conventions in our microscope and image processing procedures.…”

Section: Introductionmentioning

confidence: 99%

A Method for Establishing the Handedness of Biological Macromolecules

Belnap

Olson

Baker

1997

Journal of Structural Biology

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“…1, A, bottom panel, and B). As shown previously (27)(28)(29)(30), the in vivo preparation contained two types of particles as follows: large virus-like particles (VP1-VLPs) of ϳ45 nm in diameter (Fig. 1A, bottom panel, arrows), and T ϭ 1 tiny particle of ϳ20 nm (Fig.…”

Section: Minor Capsid Protein Vp2 Promotes Assembly Of Vp1 Into Virusmentioning

confidence: 99%

The VP2/VP3 Minor Capsid Protein of Simian Virus 40 Promotes the in Vitro Assembly of the Major Capsid Protein VP1 into Particles

Kawano

Inoue

Tsukamoto

et al. 2006

Journal of Biological Chemistry

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The SV40 capsid is composed primarily of 72 pentamers of the VP1 major capsid protein. Although the capsid also contains the minor capsid protein VP2 and its amino-terminally truncated form VP3, their roles in capsid assembly remain unknown. An in vitro assembly system was used to investigate the role of VP2 in the assembly of recombinant VP1 pentamers. Under physiological salt and pH conditions, VP1 alone remained dissociated, and at pH 5.0, it assembled into tubular structures. A stoichiometric amount of VP2 allowed the assembly of VP1 pentamers into spherical particles in a pH range of 7.0 to 4.0. Electron microscopy observation, sucrose gradient sedimentation analysis, and antibody accessibility tests showed that VP2 is incorporated into VP1 particles. The functional domains of VP2 important for VP1 binding and for enhancing VP1 assembly were further explored with a series of VP2 deletion mutants. VP3 also enhanced VP1 assembly, and a region common to VP2 and VP3 (amino acids 119 -272) was required to promote VP1 pentamer assembly. These results are relevant for controlling recombinant capsid formation in vitro, which is potentially useful for the in vitro development of SV40 virus vectors. Viral capsids are highly organized protein complexes that assemble and disassemble depending on environmental conditions during the viral life cycle. An elucidation of the mechanisms of assembly and disassembly of viral capsids may greatly help in understanding these highly organized protein complexes.SV40 is a small, nonenveloped DNA tumor virus that belongs to the family Polyomaviridae. Its capsid is formed by 72 copies of pentamers of the VP1 major capsid protein (360 molecules in total) and 72 molecules of the VP2 or VP3 minor capsid proteins. VP1 pentamers are arranged in a T ϭ 7d icosahedral lattice, and the carboxyl-terminal arm of VP1 mediates inter-pentameric contacts that hold the capsid together (1-4). VP3 is an amino-terminally truncated form of VP2. One molecule of either minor capsid protein binds to the center of a VP1 pentamer through their common carboxyl-terminal region inside the virion (5-7).However, the precise molecular mechanism for virion assembly is not known.We and others have shown that the VP1 proteins of SV40 (8 -12) and of closely related viruses such as JC virus (13, 14), murine polyomavirus (8,(15)(16)(17)(18)(19), and papillomavirus (20, 21) form virus-like particles (VLPs) 2 when expressed in insect Sf9 cells from baculoviral vectors. The properties of VP1-VLPs are very similar to those of wild type virions in that they dissociate into pentamers following treatment with a calcium-chelating agent (EGTA) under reducing conditions in vitro (22-24). Previously, we prepared highly purified SV40 VP1 pentamers (9, 25, 26), which assembled into morphologically heterogeneous particles under various nonphysiological conditions (26). Such particles include T ϭ 7d (triangulation number 7 dextro) spherical particles, small T ϭ 1 (triangulation number 1) particle composed of 12 pentamers, and long tubu...

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Structure of simian virus 40 II. Symmetry and components of the virus particle

Cited by 108 publications

References 12 publications

Conserved Features in Papillomavirus and Polyomavirus Capsids

Conserved Features in Papillomavirus and Polyomavirus Capsids

A Method for Establishing the Handedness of Biological Macromolecules

The VP2/VP3 Minor Capsid Protein of Simian Virus 40 Promotes the in Vitro Assembly of the Major Capsid Protein VP1 into Particles

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