Structure and genome ejection mechanism of
            <i>Staphylococcus aureus</i>
            phage P68

Hrebik, D.; Štveráková, Dana; Škubník, Karel; Füzik, T.; Pantůček, Roman; Plevka, Pavel

doi:10.1126/sciadv.aaw7414

Cited by 53 publications

(45 citation statements)

References 60 publications

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“…The structure of RBP is remarkably similar to the "tail fiber" (gp17) of the distantly related staphylococcal podovirus P68 [37] (Fig 5C, S1 Table), presumably reflecting specificity for S. aureus surface structures. However, in P68 gp17, the stem domain is less bent at the hinge compared to 80α (66˚vs.…”

Section: Receptor Binding Protein (Rbp Gp61)mentioning

confidence: 77%

“…Host specificity is reflected in the structure of the receptor-binding structures of the infecting phages. The distantly related S. aureus-infecting podovirus P68 has a "tail fiber" protein (gp17) that is remarkably similar to the 80α RBP [37] (25% sequence identity), suggesting that this structure is conserved among phages that infect S. aureus. In contrast, phage Andhra, which is structurally very similar to P68, but infects S. epidermidis [40], has a completely different predicted RBP structure based on a β-helical architecture.…”

Section: Discussionmentioning

confidence: 99%

“…The presence of multiple copies of receptor binding complexes is a common theme among phages of Gram-positive bacteria. 80α has six trimers of RBP, while P68 has twelve [37], and lactococcal phage TP901-1 has 18 trimers of its BppL receptor binding protein [23]. Presumably, the presence of multiple copies of the receptor binding proteins increases the avidity of the low-affinity interaction with WTA and surface polysaccharides.…”

Section: Discussionmentioning

confidence: 99%

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Structure of the host cell recognition and penetration machinery of a Staphylococcus aureus bacteriophage

et al. 2020

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Staphylococcus aureus is a common cause of infections in humans. The emergence of virulent, antibiotic-resistant strains of S. aureus is a significant public health concern. Most virulence and resistance factors in S. aureus are encoded by mobile genetic elements, and transduction by bacteriophages represents the main mechanism for horizontal gene transfer. The baseplate is a specialized structure at the tip of bacteriophage tails that plays key roles in host recognition, cell wall penetration, and DNA ejection. We have used high-resolution cryo-electron microscopy to determine the structure of the S. aureus bacteriophage 80α baseplate at 3.75 Å resolution, allowing atomic models to be built for most of the major tail and baseplate proteins, including two tail fibers, the receptor binding protein, and part of the tape measure protein. Our structure provides a structural basis for understanding host recognition, cell wall penetration and DNA ejection in viruses infecting Gram-positive bacteria. Comparison to other phages demonstrates the modular design of baseplate proteins, and the adaptations to the host that take place during the evolution of staphylococci and other pathogens. Author summaryThe emergence of virulent strains of Staphylococcus aureus that are resistant to most antibiotics has become a major public health concern. Virulence and resistance determinants in S. aureus are usually carried on mobile genetic elements (MGEs). Transduction by bacteriophages provides the main means by which MGEs are disseminated horizontally through the bacterial population, and is therefore essential to the evolution of pathogenicity of S. aureus and other pathogens. The baseplate is a complex structure at the tip of bacteriophage tails that serves multiple roles, including host recognition and binding, cell wall penetration, and ejection of the phage DNA. We have determined the structure of the baseplate from bacteriophage 80α, a representative of phages involved in host pathogenicity and in the mobilization of MGEs in S. aureus. Our structure provides a basis for understanding host recognition and infection by phages infecting Gram-positive hosts, and the PLOS Pathogens | https://doi.

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Section: Receptor Binding Protein (Rbp Gp61)mentioning

confidence: 77%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Structure of the host cell recognition and penetration machinery of a Staphylococcus aureus bacteriophage

et al. 2020

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“…NATURE COMMUNICATIONS | https://doi.org/10.1038/s41467-020-15575-4 ARTICLE Analysis of the recently published, in situ 12-fold-averaged cryo-EM reconstructions of the portals of phages phi29 16 , P23-45 17 , P68 44 , and herpes simplex virus 1 15 , suggests that the portal morphing likely occurs in many other viruses. Because of the 12fold averaging, these reconstructions can resolve only those parts of the portal structure, which obey the 12-fold symmetry, whereas the symmetry-mismatched capsid-portal interface is not resolved.…”

Section: Discussionmentioning

confidence: 99%

“…We found that the N-terminal portal regions are not resolved in all these reconstructions. Also, in the P68 portal 44 , there is the long unresolved loop formed by residues 84-103, located in the periphery of the wing domain. Since these unresolved portal regions do not obey the 12-fold symmetry, they probably interact with the capsid and morph to compensate for the symmetry mismatch.…”

Section: Discussionmentioning

confidence: 99%

Structural morphing in a symmetry-mismatched viral vertex

et al. 2020

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Large biological structures are assembled from smaller, often symmetric, sub-structures. However, asymmetry among sub-structures is fundamentally important for biological function. An extreme form of asymmetry, a 12-fold-symmetric dodecameric portal complex inserted into a 5-fold-symmetric capsid vertex, is found in numerous icosahedral viruses, including tailed bacteriophages, herpesviruses, and archaeal viruses. This vertex is critical for driving capsid assembly, DNA packaging, tail attachment, and genome ejection. Here, we report the near-atomic in situ structure of the symmetry-mismatched portal vertex from bacteriophage T4. Remarkably, the local structure of portal morphs to compensate for symmetry-mismatch, forming similar interactions in different capsid environments while maintaining strict symmetry in the rest of the structure. This creates a unique and unusually dynamic symmetry-mismatched vertex that is central to building an infectious virion.

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