2019
DOI: 10.1038/s41564-019-0477-7
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Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres

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Cited by 59 publications
(54 citation statements)
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“…Structural sequence analysis predicted that the depolymerase activity of these phages resides in tailspikes. Tail fibers and tailspikes are responsible of specific recognition of bacterial surfaces [18], and depolymerases have been shown to participate in this process [19]. The fact that all four phages shared similar depolymerases may explain why they infect the same capsular type.…”
Section: Discussionmentioning
confidence: 99%
“…Structural sequence analysis predicted that the depolymerase activity of these phages resides in tailspikes. Tail fibers and tailspikes are responsible of specific recognition of bacterial surfaces [18], and depolymerases have been shown to participate in this process [19]. The fact that all four phages shared similar depolymerases may explain why they infect the same capsular type.…”
Section: Discussionmentioning
confidence: 99%
“…Our evidence of ORF31 as being the putative tail fiber is based on the level of structural similarity to tail fiber of bacteriophage Mu G+. A recent crystal structure showed that the tail fiber and the chaperone of Mu form a complex and that both proteins are part of the mature virion [37]. However, none of the two chaperones of S144 were identified in the proteome analysis, suggesting that they are not part of the mature virion.…”
Section: Discussionmentioning
confidence: 99%
“…The genes for the tail fiber morphogenesis include the tail fiber protein (ORF31) and two chaperones (ORF32 and ORF33), which are predicted to be needed for tail fiber assembly, as both proteins showed high homology to GpU, the chaperone of the tail fiber protein of Mu G+ (HHPRED probability 100%, e-value: 1.3 −43 ). The structural prediction of ORF31 using PHYRE2 (99.8% confidence), SWISS-MODEL (QMEAN: −3.59) and HHPRED (98.13%, e-value: 2.1e −8 ) indicated homology to the tail fiber from bacteriophage Mu G+ (gpS), more specific the distal C-terminus (amino acids 351-449) responsible for receptor binding [37]. As evident from the superimposed alignment in Figure 3, the PHYRE2 structure prediction of ORF31 aligned exquisitely with the structure of gpS, even though they only share 21.55% identity at the amino acid level.…”
Section: Product Functional Category Clustermentioning
confidence: 99%
“…Such changes lead to altered structural gene products, for example, encoding phage tail fiber assembly proteins that are necessary for phage attachment to the host cell or adsorption, which is the first step of phage infection. Adaptation can also reduce lysis time and increase phage burst size [ 43 , 44 ]. Recent findings on the Eliava Staphylococcal Bacteriophage cocktail that consist of Twort-like phage Sb-1 showed that after the adaptation process, newly formed phage clones were found in phage stock, and such a process increased phage lytic activity from 87% to 96% on globally diverse S. aureus strains.…”
Section: Discussionmentioning
confidence: 99%