P22 Coat Protein Structures Reveal a Novel Mechanism for Capsid Maturation: Stability without Auxiliary Proteins or Chemical Crosslinks

Parent, Kristin N.; Khayat, Reza; Tu, Long; Suhanovsky, Margaret M.; Cortines, Juliana R.; Teschke, Carolyn M.; Johnson, John E.; Baker, Timothy S.

doi:10.1016/j.str.2009.12.014

Cited by 137 publications

(291 citation statements)

References 68 publications

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“…3A), which makes them more parallel to the shell surface. A similar relative movement between the A-and P-domains has previously been found in the maturation of HK97 (46) and P22 (20). Monomers were rearranged in the capsomers of the head relative to the prohead.…”

Section: Structure Of the T7 Capsid Shell From Cryo-electronsupporting

confidence: 78%

“…In summary, our results indicate that the maturation of T7 is more similar to the maturation mechanism of HK97 than to the maturation in P22-like systems (20). Nevertheless, as no chemical cross-linking is involved in T7 maturation, it could be speculated that T7 represents the most basic system of capsid maturation.…”

Section: Structure Of the T7 Capsid Shell From Cryo-electronmentioning

confidence: 65%

“…The existence of three transformation mechanisms to acquire shell stability has been recently reviewed (20). The most common mechanism is the incorporation of accessory proteins that establish an additional set of contacts to reinforce those built by the main shell protein in the prohead.…”

mentioning

confidence: 99%

“…A second mechanism involves the generation of new interactions between neighboring subunits by using additional domains inserted within the primitive protein sequence. This strategy is employed by phages 29 (15) and P22, in which the presence of an inserted domain with a telokin Ig-like fold has been related to a direct assembly of the capsid from monomeric subunits instead of intermediate capsomeric subassemblies (20). The third mechanism, which appears to be unique to HK97, involves the formation of covalent intersubunit cross-linking, leading to extensive interlocking of the shell in a giant superstructure (26).…”

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confidence: 99%

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Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7

Ionel

Velázquez-Muriel

Luque

et al. 2011

Journal of Biological Chemistry

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Maturation of dsDNA bacteriophages involves assembling the virus prohead from a limited set of structural components followed by rearrangements required for the stability that is necessary for infecting a host under challenging environmental conditions. Here, we determine the mature capsid structure of T7 at 1 nm resolution by cryo-electron microscopy and compare it with the prohead to reveal the molecular basis of T7 shell maturation. The mature capsid presents an expanded and thinner shell, with a drastic rearrangement of the major protein monomers that increases in their interacting surfaces, in turn resulting in a new bonding lattice. The rearrangements include tilting, in-plane rotation, and radial expansion of the subunits, as well as a relative bending of the A-and P-domains of each subunit. The unique features of this shell transformation, which does not employ the accessory proteins, inserted domains, or molecular interactions observed in other phages, suggest a simple capsid assembling strategy that may have appeared early in the evolution of these viruses.

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Section: Structure Of the T7 Capsid Shell From Cryo-electronsupporting

confidence: 78%

Section: Structure Of the T7 Capsid Shell From Cryo-electronmentioning

confidence: 65%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7

Ionel

Velázquez-Muriel

Luque

et al. 2011

Journal of Biological Chemistry

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“…The I domain of T4 is smaller than the I domain of phi812, and is not in contact with minor capsid Soc proteins positioned around the quasi-threefold axes of the capsid (41,42). Furthermore, the coat protein of Podoviridae bacteriophage P22 contains an inserted telokin-like domain that was speculated to stabilize the overall fold of the P22 coat protein monomer (43). However, the inserted domain of P22 is built from several α-helices and does not resemble the I domain of phi812.…”

Section: Significancementioning

confidence: 99%

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Nováček

Šiborová

Benešík

et al. 2016

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

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Bacteriophages from the family Myoviridae use double-layered contractile tails to infect bacteria. Contraction of the tail sheath enables the tail tube to penetrate through the bacterial cell wall and serve as a channel for the transport of the phage genome into the cytoplasm. However, the mechanisms controlling the tail contraction and genome release of phages with “double-layered” baseplates were unknown. We used cryo-electron microscopy to show that the binding of the Twort-like phage phi812 to the Staphylococcus aureus cell wall requires a 210° rotation of the heterohexameric receptor-binding and tripod protein complexes within its baseplate about an axis perpendicular to the sixfold axis of the tail. This rotation reorients the receptor-binding proteins to point away from the phage head, and also results in disruption of the interaction of the tripod proteins with the tail sheath, hence triggering its contraction. However, the tail sheath contraction of Myoviridae phages is not sufficient to induce genome ejection. We show that the end of the phi812 double-stranded DNA genome is bound to one protein subunit from a connector complex that also forms an interface between the phage head and tail. The tail sheath contraction induces conformational changes of the neck and connector that result in disruption of the DNA binding. The genome penetrates into the neck, but is stopped at a bottleneck before the tail tube. A subsequent structural change of the tail tube induced by its interaction with the S. aureus cell is required for the genome’s release.

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Bacteriophages: Structure

Cuervo

Carrascosa

2012

Encyclopedia of Life Sciences

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Bacterial viruses, or bacteriophages, are ubiquitous organisms spanning very different ecological niches. Although genome comparison fails to show extensive relationship among bacteriophages, recent structural studies reveal a high degree of similarities. Most bacteriophages present an icosahedral proteinaceous head, which contains the nucleic acid, either deoxyribonucleic acid (DNA) or ribonucleic acid (RNA) . Exceptions to this rule are few cases where a lipid envelope forms part of the head, and those other cases where the head presents a filamentous geometry. The way bacteriophages infect the host cell is the basis of a main difference among them: one group (Caudovirales) has a specialised structure (the tail) that is responsible for the recognition of the host cell and the viral genome delivery, whereas those bacteriophages without tail present a variety of infecting strategies. In this study we will deal with the main common characteristics of bacteriophage heads and tails supporting their common evolutionary origin. Key Concepts: Bacteriophages share extended structural and functional similarities. Bacteriophages are excellent examples of optimisation of genetic information to carry out complex functions. Most bacteriophages enclose their nucleic acid in a protein container (built by multiple copies of one (or a few) proteins), and in a few cases they may include lipid envelopes. The most conserved geometry in bacteriophage heads is icosahedral. Double stranded DNA icosahedral bacteriophages follow a common assembly pathway. The Caudovirales group (bacteriophages with icosahedral heads, dsDNA and a tail) are the most abundant virus type. The packaging of dsDNA inside Caudovirales requires energy conversion (ATP hydrolysis) into mechanical translocation, and it is carried out by a dedicated viral machinery. The maturation of icosahedral proheads into viral heads involves drastic reorganisations of the capsid components leading to more stable particles. The tail of Caudovirales is a sophisticated machinery involved in cell recognition and nucleic acids delivery. There are three main architectural designs of bacteriophage tails, each one adapting to different host interaction strategies.

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P22 Coat Protein Structures Reveal a Novel Mechanism for Capsid Maturation: Stability without Auxiliary Proteins or Chemical Crosslinks

Cited by 137 publications

References 68 publications

Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7

Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Bacteriophages: Structure

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