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

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structure of the host cell recognition and penetration machinery of a Staphylococcus aureus bacteriophage
Creator	Dearborn, Altaira Dokland Id, Terje Kizziah Id, James Manning Id, Keith
Source	PMC
abstract	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.
has issue date	2020-02-18(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1008314
bibo:pmid	32069326
has license	cc0
sha1sum (hex)	3e7042ac51bcdbd64db05d998292e8ed45ebfc07
schema:url	https://doi.org/10.1371/journal.ppat.1008314
resource representing a document's title	Structure of the host cell recognition and penetration machinery of a Staphylococcus aureus bacteriophage
has PubMed Central identifier	PMC7048315
has PubMed identifier	32069326
schema:publication	PLoS Pathog
resource representing a document's body	covid:3e7042ac51bcdbd64db05d998292e8ed45ebfc07#body_text
is schema:about of	covid:arg/3e7042ac51bcdbd64db05d998292e8ed45ebfc07 named entity 'virulence' named entity 'bacteriophages' named entity 'pathogens' named entity 'S. aureus' named entity 'cell wall' named entity 'S. aureus' named entity 'cryo-electron microscopy' named entity 'viruses' named entity 'S. aureus' named entity 'polymerization' named entity 'mitomycin' named entity 'phage' named entity 'icosahedral capsid' named entity 'S. aureus' named entity 'coiled coil' named entity 'adsorption' named entity 'S. aureus' named entity 'previously identified' named entity 'hydrolase' named entity 'protein' named entity 'genetic material' named entity 'Staphylococcus epidermidis' named entity 'hexameric' named entity 'FibL' named entity 'RMSD' named entity 'protein' named entity 'β-sandwich' named entity 'hydrolase' named entity 'ORFs' named entity 'α-helical' named entity 'highly conserved' named entity 'Podoviridae' named entity 'protein' named entity 'coiled-coil' named entity 'tightly regulated' named entity 'β-sandwich' named entity 'trimeric protein' named entity 'phage' named entity 'FibL' named entity '4.2' named entity 'protein' named entity 'genomes' named entity 'FibL' named entity 'tube domain' named entity 'phage' named entity 'FibL' named entity 'Ig-like' named entity 'highly conserved' named entity 'FibL' named entity 'phage' named entity 'proximal' named entity 'HHpred' named entity 'phages' named entity 'C-terminus' named entity 'Host specificity' named entity 'conformational change' named entity 'protein complexes' named entity 'gene' named entity 'coagulase-negative staphylococci' named entity 'phages' named entity 'phages' named entity 'lumen' named entity 'Listeria monocytogenes' named entity 'evolution' named entity 'therapeutic strategies' named entity 'receptor binding' named entity 'hydrophobicity' named entity 'S4G' named entity 'immunoglobulin-like' named entity 'columns 3' named entity 'S. aureus' named entity 'S. aureus' named entity 'lysogen' named entity 'phages' named entity 'WTA' named entity 'infection' named entity 'real-space'

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