Diversity and Function of Phage Encoded Depolymerases

Knecht, Leandra E.; Veljkovic, Marjan; Fieseler, Lars

doi:10.3389/fmicb.2019.02949

Cited by 216 publications

(194 citation statements)

References 76 publications

(152 reference statements)

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“…Previously, the homologous of ORF09 of the highly related phage SE4 was proposed to encode an additional tail fiber [35]. However, the structure prediction of the analogous gene in S144 (ORF17) using PHYRE2 did not resemble a tail spike or a tail fiber (data not shown) and ORF17 is thus annotated as a tail protein, even though HHPRED predicts that it might have the hydrolase activity seen in some tail spikes [36]. 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+.…”

Section: Discussionmentioning

confidence: 94%

“…Of the four tail proteins, ORF17 has been annotated as a tail fiber protein in the Salmonella phages SE4 and SE13 [35]. Although HHPRED predicts that ORF17 may have hydrolase activity as seen in some tail spikes [36], the PHYRE2 structure prediction did not resemble neither a tail spike, nor a tail fiber (data not shown) and is therefore annotated simply as a tail protein. ORF24 and ORF25 have no similarities with any described genes or proteins, but we suggest they may code for other structural proteins, since they have been identified by ESI-MS/MS and are located in between the genes encoding tail and baseplate proteins.…”

Section: Product Functional Category Clustermentioning

confidence: 99%

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Phage S144, a New Polyvalent Phage Infecting Salmonella spp. and Cronobacter sakazakii

Gambino

Sørensen

Ahern

et al. 2020

IJMS

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Phages are generally considered species- or even strain-specific, yet polyvalent phages are able to infect bacteria from different genera. Here, we characterize the novel polyvalent phage S144, a member of the Loughboroughvirus genus. By screening 211 Enterobacteriaceae strains, we found that phage S144 forms plaques on specific serovars of Salmonella enterica subsp. enterica and on Cronobacter sakazakii. Analysis of phage resistant mutants suggests that the O-antigen of lipopolysaccharide is the phage receptor in both bacterial genera. The S144 genome consists of 53,628 bp and encodes 80 open reading frames (ORFs), but no tRNA genes. In total, 32 ORFs coding for structural proteins were confirmed by ESI-MS/MS analysis, whereas 45 gene products were functionally annotated within DNA metabolism, packaging, nucleotide biosynthesis and phage morphogenesis. Transmission electron microscopy showed that phage S144 is a myovirus, with a prolate head and short tail fibers. The putative S144 tail fiber structure is, overall, similar to the tail fiber of phage Mu and the C-terminus shows amino acid similarity to tail fibers of otherwise unrelated phages infecting Cronobacter. Since all phages in the Loughboroughvirus genus encode tail fibers similar to S144, we suggest that phages in this genus infect Cronobacter sakazakii and are polyvalent.

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Section: Discussionmentioning

confidence: 94%

Section: Product Functional Category Clustermentioning

confidence: 99%

Phage S144, a New Polyvalent Phage Infecting Salmonella spp. and Cronobacter sakazakii

Gambino

Sørensen

Ahern

et al. 2020

IJMS

View full text Add to dashboard Cite

show abstract

“…This is in contrast to phage HP3 which showed no halo formation (picture above Figure 4Di). This halo formation is indicative of EPS (extracellular polymetric substance)-degrading activity (Knecht, Veljkovic and Fieseler, 2020).…”

Section: Phage Es17 May Bind Bacterial Polysaccharidesmentioning

confidence: 99%

Targeting of Mammalian Glycans Enhances Phage Predation in the Gastrointestinal Tract

Green

Liu

et al. 2020

Preprint

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The human mucosal surface is a complex ecosystem comprised of a eukaryotic epithelium, a prokaryotic microbiota, and a carbohydrate-rich interface that separates them. A less characterized, third entity, that of bacteriophage (phage), parasitizes prokaryotes but generally do not interact with eukaryotic cells. In the gastrointestinal tract, the interaction of these two domains of life influences the health status of the host, especially if there is colonization with invasive pathobionts. If the pathobiont causes a symptomatic infection, treatment with antibiotics is necessary. However, antibiotics act broadly thereby killing many protective commensals and they lack the physio-chemical properties to be optimally active in the mucosa, and may have associated adverse effects, including toxicities. Here, we report a novel C3 type phage of the genus Kuravirus whose lytic cycle is enhanced in intestinal environments. The enhanced activity is encoded in the viral tail fiber gene, whose protein product binds human heparan sulfated proteoglycans and localizes the phage to the epithelial cell surface, thereby positioning it near the location of its bacterial host. This finding offers the prospect of developing epithelial-targeting phage to selectively remove invasive pathobiont species from mucosal surfaces.

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“…Overall, a limited number of enzymes in active particular capsular types have been described [16]. In addition to their potential therapeutic applications, phage-borne depolymerases have been suggested for capsular typing [17]. For these reasons, discovering new Klebsiella phage depolymerases against distinct capsular types is an interesting topic with potential biomedical applications.…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of Two Klebsiella pneumoniae Phages Encoding Divergent Depolymerases

Domingo‐Calap

Beamud

Mora-Quilis

et al. 2020

IJMS

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The emergence of multidrug-resistant bacteria is a major global health concern. The search for new therapies has brought bacteriophages into the spotlight, and new phages are being described as possible therapeutic agents. Among the bacteria that are most extensively resistant to current antibiotics is Klebsiella pneumoniae, whose hypervariable extracellular capsule makes treatment particularly difficult. Here, we describe two new K. pneumoniae phages, πVLC5 and πVLC6, isolated from environmental samples. These phages belong to the genus Drulisvirus within the family Podoviridae. Both phages encode a similar tail spike protein with putative depolymerase activity, which is shared among other related phages and probably determines their ability to specifically infect K. pneumoniae capsular types K22 and K37. In addition, we found that phage πVLC6 also infects capsular type K13 and is capable of striping the capsules of K. pneumoniae KL2 and KL3, although the phage was not infectious in these two strains. Genome sequence analysis suggested that the extended tropism of phage πVLC6 is conferred by a second, divergent depolymerase. Phage πVLC5 encodes yet another putative depolymerase, but we found no activity of this phage against capsular types other than K22 and K37, after testing a panel of 77 reference strains. Overall, our results confirm that most phages productively infected one or few Klebsiella capsular types. This constitutes an important challenge for clinical applications.

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Diversity and Function of Phage Encoded Depolymerases

Cited by 216 publications

References 76 publications

Phage S144, a New Polyvalent Phage Infecting Salmonella spp. and Cronobacter sakazakii

Phage S144, a New Polyvalent Phage Infecting Salmonella spp. and Cronobacter sakazakii

Targeting of Mammalian Glycans Enhances Phage Predation in the Gastrointestinal Tract

Isolation and Characterization of Two Klebsiella pneumoniae Phages Encoding Divergent Depolymerases

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