Structural Transitions During Maturation of Bacteriophage Lambda Capsids

Dokland, Terje; Murialdo, Helios

doi:10.1006/jmbi.1993.1545

Cited by 163 publications

(147 citation statements)

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“…The profile topographies of the particles (Fig. 2) are consistent with the dimensions previously obtained by cryo-electron microscopy 19,20 , indicating that the particles are not significantly affected by the interaction with the HOPG surface upon adsorption.…”

Section: Resultssupporting

confidence: 87%

“…Although the gpD protein is not required for DNA translocation into the capsid, it is essential for the packaging of the penultimate 8-10 kbp of the viral genome 22 . This finding has been interpreted to indicate that gpD provides to the capsid sufficient structural stability to support the tens of atmospheres internal pressure generated by the packed dsDNA 19,20 . Structural data indicate that gpD monomers assemble as a trimer spike at the threefold axes of the expanded shell.…”

Section: Discussionmentioning

confidence: 94%

“…This nucleates the assembly of 405 copies of major protein gpE, into an icosahedral shell with a T ¼ 7 triangulation number, chaperoned by the gpNu3 scaffolding protein. Upon packaging B15 kb of DNA, the shell undergoes an expansion transition that exposes hydrophobic surface area to which the gpD cementing protein adds 19,20 . The immature capsid is 4 nm thick and 50 nm in diameter, whereas the mature capsid is thin (2 nm) and presents an angularized icosahedral shape of B65 nm in diameter that can accommodate the 48.5 kbp dsDNA genome.…”

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confidence: 99%

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Cementing proteins provide extra mechanical stabilization to viral cages

et al. 2014

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The study of virus shell stability is key not only for gaining insights into viral biological cycles but also for using viral capsids in materials science. The strength of viral particles depends profoundly on their structural changes occurring during maturation, whose final step often requires the specific binding of 'decoration' proteins (such as gpD in bacteriophage lambda) to the viral shell. Here we characterize the mechanical stability of gpD-free and gpD-decorated bacteriophage lambda capsids. The incorporation of gpD into the lambda shell imparts a major mechanical reinforcement that resists punctual deformations. We further interrogate lambda particle stability with molecular fatigue experiments that resemble the sub-lethal Brownian collisions of virus shells with macromolecules in crowded environments. Decorated particles are especially robust against collisions of a few k B T (where k B is the Boltzmann's constant and T is the temperature B300 K), which approximate those anticipated from molecular insults in the environment.

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Section: Resultssupporting

confidence: 87%

Section: Discussionmentioning

confidence: 94%

mentioning

confidence: 99%

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Cementing proteins provide extra mechanical stabilization to viral cages

et al. 2014

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“…The PFT method has been used by us as well as others to determine the structures of several icosahedral viruses (e.g., Dokland and Murialdo, 1993;Cheng et al, 1994aCheng et al, ,b, 1995Hagensee et al, 1994;Kenney et al, 1994;Venién-Bryan and Fuller, 1994;Wikoff et al, 1994;Fuller et al, 1995;Ilag et al, 1995;Zhao et al, 1995). The method could also be adapted for the analysis of asymmetric macromolecules or those with lower symmetry than an icosahedron.…”

Section: Introductionmentioning

confidence: 99%

A Model-Based Approach for Determining Orientations of Biological Macromolecules Imaged by Cryoelectron Microscopy

Baker

Cheng

1996

Journal of Structural Biology

362

226

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“…The most detailed structural information on dsDNA bacteriophage capsids has been determined by cryo-electron microscopy and image reconstruction (Conway et al, 1995;Dokland et al, 1992;Dokland & Murialdo, 1993;Prasad et al, 1993). Bacteriophage structure has also been investigated by X-ray solution scattering (King et al, 1976;Stroud et al, 1981) and spectroscopy (Li et al, 1981;Prevelige et al, 1993;Steven et al, 1990;Thomas et al, 1982).…”

Section: Introductionmentioning

confidence: 99%

Crystallographic analysis of the dsDNA bacteriophage HK97 mature empty capsid

Wikoff

Duda

Hendrix

et al. 1999

Acta Crystallogr D Biol Cryst

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HK97 is a member of the Siphovirus family of dsDNA bacteriophages. It is similar in architecture to bacteriophage !, the type member of this family, with an icosahedral capsid of triangulation number T = 7. No high-resolution structural information is available for the dsDNA phages, and HK97 is the only dsDNA bacteriophage capsid to produce crystals which diffract X-rays. At 650 A Ê in diameter, the large size of the particle and resultant large unit cell create crystallographic challenges. The empty Head II (mature) particles were expressed in Escherichia coli and assembled in vitro, but they have the same morphology as the mature HK97 capsid. Previously reported Head II crystals diffracting to 3.5 A Ê resolution are examined here in detail. Although the cell dimensions suggest an orthorhombic lattice, further analysis demonstrated that the space group was monoclinic. This has been con®rmed by the present study. Images were recorded on the F1 beamline at CHESS and they were processed and scaled, resulting in a data set with a cumulative completeness of 65% and a scaling R factor of 7.7% to 7 A Ê . The cell dimensions after post-re®nement were a = 580, b = 626, c = 788 A Ê , = 90.0 . From the particle dimensions determined by cryo-electron microscopy (cryo-EM), there were determined to be two particles per unit cell. Systematic absences of even re¯ections along the 0k0 lattice line indicate that the space group is P2 1 . The rotation function was used to determine the orientation of the particles in the unit cell and to con®rm the space group. An icosahedral twofold axis is approximately, but not exactly, aligned with the crystallographic screw (b) axis. An icosahedral twofold axis orthogonal to the one approximately parallel to the b axis, is rotated 18 away from the a axis. The centers of the two particles must be positioned close to the minimum-energy packing arrangement for spheres, which places one particle at ( 1 4 , 0, 1 4 ) and the other particle at ( 3 4 , 1 2 , 3 4 ). The particle position and orientation were con®rmed by calculating a Patterson function. The particles interact closely along icosahedral threefold axes, which occurs both along the crystallographic a axis and along the b axis. The particle dimensions derived from this packing arrangement agree well with those determined by cryo-EM and image reconstruction. The cryo-EM reconstruction will be used as a model to initiate phase determination; structure determination at 7 A Ê is under way.

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Structural Transitions During Maturation of Bacteriophage Lambda Capsids

Cited by 163 publications

References 0 publications

Cementing proteins provide extra mechanical stabilization to viral cages

Cementing proteins provide extra mechanical stabilization to viral cages

A Model-Based Approach for Determining Orientations of Biological Macromolecules Imaged by Cryoelectron Microscopy

Crystallographic analysis of the dsDNA bacteriophage HK97 mature empty capsid

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