Functional and structural dissection of the tape measure protein of lactococcal phage TP901-1

Mahony, Jennifer; Alqarni, Mona; Stockdale, Stephen R.; Spinelli, S.; Feyereisen, Marine; Cambillau, Christian; Sinderen, Douwe van

doi:10.1038/srep36667

“…Although not conclusively determined, this density matched the C-terminal residues 1135-1154 of TMP. TMP is the only protein known to fill the tail channel and the localization of its C-terminus at the baseplate agrees with previous research on other phages (35). Additional density attributable to TMP could be seen inside the tail lumen, but was not interpretable in terms of the atomic structure ( Fig.…”

Section: Tail-associated Lysin (Tal Gp59) and Tape Measure Protein (supporting

confidence: 89%

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

Kizziah

¹

,

Manning

²

,

Dearborn

³

et al. 2019

Preprint

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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 3.7 Å resolution, allowing atomic models to be built for most of the major tail and baseplate proteins, including two tail fibers, a trimeric 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 demonstrate the modular design of baseplate proteins, and the adaptations to the host that take place during the evolution of staphylococci and other pathogens.

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“…The TMP triplet fit into a hydrophobic patch on Tal (Fig 4G and 4H). The localization of the TMP C-terminus at the baseplate agrees with previous research on other phages [36]. Additional density attributable to TMP could be seen inside the tail lumen, but was not interpretable in terms of the atomic structure ( Fig 4B).…”

Section: Tail-associated Lysin (Tal Gp59) and Tape Measure Protein (supporting

confidence: 87%

“…Once the peptidoglycan layer is degraded and Tal reaches the plasma membrane, the αhelices in the plug and rod must be removed to permit extrusion of the pore-forming TMP ( Fig 6C) [36]. This conformational change is fundamentally different from the opening of the p2 baseplate [26].…”

Section: Discussionmentioning

confidence: 99%

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

Kizziah

¹

,

Manning

²

,

Dearborn

³

et al. 2020

View full text Add to dashboard Cite

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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“…Such an interpretation is corroborated by evidence that phage P1532, heatstable up to 90°C, shows an even shorter protein composed by 916 amino acids. TMPs of phages infecting Lactococcus strains have hydrophobic regions that assemble in transmembrane-spanning domains that serve different functions for phage infectivity including the recruitment of chaperones (82). These features, associated with heat-stability as it is the case for phage CB19, may represent an interesting starting point to harness the power of phage-derived, heat-stable proteins to interact with membrane-spanning receptors involved in mitogenic signal transduction.…”

Section: Discussionmentioning

confidence: 99%

Phage composition of a fermented milk and colostrum product assessed by microbiome array; putative role of open reading frames in reference to cell signaling and neurological development

Pacini¹,

Ruggiero²

2019

Preprint

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Bacteriophages (phages), Earth's most numerous biological entities, are natural constituents of alimentary matrices; in this study we describe the characterization of phage populations in a product obtained by fermentation of bovine milk and colostrum. Such characterizations were achieved using a microarray consisting of a chip covered in short DNA sequences that are specific to certain target organisms for a total of approximately 12,000 species. The only viruses evidenced by the array belonged to Siphoviridae, the largest phage family that targets bacteria and archea. The array yielded 27 iterations corresponding to a unique target. We discuss the putative role of some open reading frames of these phages in conferring health-supporting properties.

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Functional and structural dissection of the tape measure protein of lactococcal phage TP901-1

Cited by 89 publications

References 44 publications

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

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

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

Phage composition of a fermented milk and colostrum product assessed by microbiome array; putative role of open reading frames in reference to cell signaling and neurological development

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