The DNA-packaging nanomotor of tailed bacteriophages

Casjens, Sherwood

doi:10.1038/nrmicro2632

Cited by 223 publications

(246 citation statements)

References 169 publications

Supporting

Mentioning

243

Contrasting

Order By: Relevance

“…Packaging is initiated by the two-subunit terminase, which recognizes and specifically cleaves target DNA (15)(16)(17). Phage and SaPI both use the phage-encoded large (TerL) subunit, and this is complexed with a phage-or SaPI-encoded small subunit (TerS P or TerS S , respectively), which determines packaging specificity (9,12).…”

Section: Resultsmentioning

confidence: 99%

Staphylococcal pathogenicity island interference with helper phage reproduction is a paradigm of molecular parasitism

Ram

Chen

Kumar

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

120

135

View full text Add to dashboard Cite

Staphylococcal pathogenicity islands (SaPIs) carry superantigen and resistance genes and are extremely widespread in Staphylococcus aureus and in other Gram-positive bacteria. SaPIs represent a major source of intrageneric horizontal gene transfer and a stealth conduit for intergeneric gene transfer; they are phage satellites that exploit the life cycle of their temperate helper phages with elegant precision to enable their rapid replication and promiscuous spread. SaPIs also interfere with helper phage reproduction, blocking plaque formation, sharply reducing burst size and enhancing the survival of host cells following phage infection. Here, we show that SaPIs use several different strategies for phage interference, presumably the result of convergent evolution. One strategy, not described previously in the bacteriophage microcosm, involves a SaPI-encoded protein that directly and specifically interferes with phage DNA packaging by blocking the phage terminase small subunit. Another strategy involves interference with phage reproduction by diversion of the vast majority of virion proteins to the formation of SaPI-specific small infectious particles. Several SaPIs use both of these strategies, and at least one uses neither but possesses a third. Our studies illuminate a key feature of the evolutionary strategy of these mobile genetic elements, in addition to their carriage of important genes—interference with helper phage reproduction, which could ensure their transferability and long-term persistence.

show abstract

Section: Resultsmentioning

confidence: 99%

Staphylococcal pathogenicity island interference with helper phage reproduction is a paradigm of molecular parasitism

Ram

Chen

Kumar

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

120

135

View full text Add to dashboard Cite

show abstract

“…Tailed bacteriophages and the evolutionarily related herpesviruses package their genomes into preformed empty procapsids using a molecular motor embedded in one of the fivefold-symmetrical vertices of the icosahedral viral shell (Casjens, 2011). There are two general mechanisms of packaging concatemeric viral double-stranded DNA.…”

Section: Introductionmentioning

confidence: 99%

The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding

Benini

Chechik

Lombardia

et al. 2013

Acta Crystallogr F Struct Biol Cryst Commun

View full text Add to dashboard Cite

PDB Reference: DNA-binding domain of the bacteriophage SF6 small terminase subunit, 2cmp DNA packaging in tailed bacteriophages and in evolutionarily related herpesviruses is controlled by a viral-encoded terminase. As in a number of other phages, in the Bacillus subtilis bacteriophages SF6 and SPP1 the terminase complex consists of two proteins: G1P and G2P. The crystal structure of the N-terminal DNA-binding domain of the bacteriophage SF6 small terminase subunit G1P is reported. Structural comparison with other DNA-binding proteins allows a general model for the interaction of G1P with the packaginginitiation site to be proposed.

show abstract

“…Procapsids are typically constructed of a few quasiequivalent proteins that self-assemble into an icosahedral shell aided by a scaffolding protein [3][4][5] . The portal complex is assembled at a unique vertex to provide a canal for DNA entry and release during packing and infection, respectively 6 . DNA packaging triggers a major re-organization of the proteins assembled into the procapsid.…”

mentioning

confidence: 99%

Cementing proteins provide extra mechanical stabilization to viral cages

et al. 2014

View full text Add to dashboard Cite

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.

show abstract

The DNA-packaging nanomotor of tailed bacteriophages

Cited by 223 publications

References 169 publications

Staphylococcal pathogenicity island interference with helper phage reproduction is a paradigm of molecular parasitism

Staphylococcal pathogenicity island interference with helper phage reproduction is a paradigm of molecular parasitism

The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding

Cementing proteins provide extra mechanical stabilization to viral cages

Contact Info

Product

Resources

About