Polysaccharide Depolymerase Associated with Bacteriophage Infection

Bartell, Pasquale F.; Orr, Thomas E.; Lam, Grace K. H.

doi:10.1128/jb.92.1.56-62.1966

Cited by 52 publications

(36 citation statements)

References 22 publications

(16 reference statements)

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“…The one Ps. aeruginosa phage depolymerase described so far (Bartell et al 1966) decreased the viscosity of slime exopolysaccharide produced by the host strain and released monomeric sugars from the substrate; it was active against polymers from a limited number of Ps. aeruginosa strains and the enzyme activity resided in a 180 000 kDa component (Bartell et al 1968) that is likely to be a particulate component of the phage tail spike assemblage consisting of either three or six enzyme subunits (Sutherland 1977).…”

Section: Discussionmentioning

confidence: 99%

Bacteriophage-derived enzyme that depolymerizes the alginic acid capsule associated with cystic fibrosis isolates ofPseudomonas aeruginosa

Glonti

Chanishvili

Taylor³

2010

Journal of Applied Microbiology

107

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Aims: To identify enzymes associated with bacteriophages infecting cystic fibrosis (CF) strains of Pseudomonas aeruginosa that are able to degrade extracellular alginic acids elaborated by the host bacterium. Methods and Results: Plaques produced by 21 Ps. aeruginosa‐specific phages were screened for the presence of haloes, an indicator of capsule hydrolytic activity. Four phages produced haloed plaques, and one (PT‐6) was investigated further. PT‐6 was shown by electron microscopy to belong to Podoviridae family C1, to reduce the viscosity of four alginate preparations using a rolling ball viscometer and to release uronic acid‐containing fragments from the polymers, as judged by spectrophotometry and thin layer chromatography. The alginase was partially purified by gel filtration chromatography and shown to be a 37 kDa polypeptide. Conclusions: Infection of CF strains of Ps. aeruginosa by phage PT‐6 involves hydrolysis of the exopolysaccharide secreted by the host. Significance and Impact of the Study: The alginase produced by PT‐6 has the potential to increase the well‐being of CF suffers by improving the surface properties of sputum, accelerating phagocytic uptake of bacteria and perturbing bacterial growth in biofilms.

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Section: Discussionmentioning

confidence: 99%

Bacteriophage-derived enzyme that depolymerizes the alginic acid capsule associated with cystic fibrosis isolates ofPseudomonas aeruginosa

Glonti

Chanishvili

Taylor³

2010

Journal of Applied Microbiology

107

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“…Organism. The bacterium used in this study, P. aeruginosa strain BI, was originally isolated from a clinical specimen and was described previously (2). GLP.…”

Section: Methodsmentioning

confidence: 99%

In vivo distribution of Pseudomonas aeruginosa slime glycolipoprotein: association with leukocytes

Lynn¹,

Sensakovic²,

Bartell³

1977

Infect Immun

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Intraperitoneal injection of slime glycolipoprotein (GLP) from Pseudomonas aeruginosa induced leukopenia and death of mice, similar to the effect of infection with viable organisms. Differential counts established that the leukopenia was characterized by a decrease in the number of polymorphonuclear leukocytes, followed by death of mice. Mice immunized with GLP survived challenge and responded with a leukocytosis that had a substantial increase in circulating polymorphonuclear leukocytes. Leukocytes from GLP-injected mice were agglutinated by anti-GLP serum, indicating an association between GLP and leukocytes. Other results indicated that 14C-labeled GLP is deposited mainly in the liver. Normal leukocytes labeled with 51Cr were injected intravenously into mice receiving an intraperitoneal injection of GLP. As with GLP, the 5'Crlabeled leukocytes were sequestered in the liver. These results indicate that GLP enters the blood stream and becomes associated mainly with neutrophils, and that the neutrophil-GLP complex is deposited in the liver, possibly accounting for the leukopenia in mice.Although infections resulting from Pseudomonas aeruginosa have been studied for many years, relatively little is known about its pathogenesis. Several possible virulence factors have been characterized, such as: proteases (11), exotoxin or toxin A (4, 12), leukocidin (13-16), and slime (1,8,18,19). The glycolipoprotein (GLP) fraction, extracted from the slime layer, has been observed to induce leukopenic and lethal effects in mice, much the same as infection with viable organisms. Active and passive immunization against highly purified GLP protected mice from leukopenia and death after challenge with live organisms (18). The production of GLP has been detected in vivo after injection of live organisms, as well as its dissemination via the peripheral blood circulation to become associated with erythrocytes (8).In this study, the GLP-induced leukopenic effect was further characterized, and the relationship between GLP and blood leukocytes was examined. The distribution of GLP in mouse organs was also determined. MATERIALS AND METHODSOrganism. The bacterium used in this study, P. aeruginosa strain BI, was originally isolated from a clinical specimen and was described previously (2). GLP. The GLP fraction was obtained from the extracellular slime layer of strain BI and was purified by the method described by Sensakovic and Bartell (18). Purified GLP was injected into mice intraperitoneally at a concentration of 50 pugIg as a challenge. This concentration represented 2 mean lethal doses and was usually lethal to 100% of the mice injected.Mice. Young, white, male Swiss mice, weighing 18 to 20 g, were used in this study. They were housed 10 per cage and supplied Purina Mouse Chow and water ad libitum. All mice were weighed immediately before injection.Mouse leukocyte counts were performed using blood samples from the tail vein. Standard techniques of dilution using 0.1 M HOl were employed followed by enumeration of the total leukocyte ...

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“…To date, some Azobacter and Pseudomonas spp. phages were found to encode alginate lyases (Bartell et al 1966;Davidson et al 1977;Glonti et al 2010), which help phages to penetrate through the acetylated poly(M)-rich EPSs produced by their bacterial hosts (Wong et al 2000;Yan et al 2014). An example of a phage with alginate-degrading activity is the P. aeruginosa phage PT-6 (Glonti et al 2010).…”

Section: Lyasesmentioning

confidence: 99%

Bacteriophage-encoded depolymerases: their diversity and biotechnological applications

Pires

Oliveira

Melo

et al. 2016

Appl Microbiol Biotechnol

361

305

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Bacteriophages (phages), natural enemies of bacteria, can encode enzymes able to degrade polymeric substances. These substances can be found in the bacterial cell surface, such as polysaccharides, or are produced by bacteria when they are living in biofilm communities, the most common bacterial lifestyle. Consequently, phages with depolymerase activity have a facilitated access to the host receptors, by degrading the capsular polysaccharides, and are believed to have a better performance against bacterial biofilms, since the degradation of extracellular polymeric substances by depolymerases might facilitate the access of phages to the cells within different biofilm layers. Since the diversity of phage depolymerases is not yet fully explored, this is the first review gathering information about all the depolymerases encoded by fully sequenced phages. Overall, in this study, 160 putative depolymerases, including sialidases, levanases, xylosidases, dextranases, hyaluronidases, peptidases as well as pectate/pectin lyases, were found in 143 phages (43 Myoviridae, 47 Siphoviridae, 37 Podoviridae, and 16 unclassified) infecting 24 genera of bacteria. We further provide information about the main applications of phage depolymerases, which can comprise areas as diverse as medical, chemical, or food-processing industry.

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Polysaccharide Depolymerase Associated with Bacteriophage Infection

Cited by 52 publications

References 22 publications

Bacteriophage-derived enzyme that depolymerizes the alginic acid capsule associated with cystic fibrosis isolates ofPseudomonas aeruginosa

Bacteriophage-derived enzyme that depolymerizes the alginic acid capsule associated with cystic fibrosis isolates ofPseudomonas aeruginosa

In vivo distribution of Pseudomonas aeruginosa slime glycolipoprotein: association with leukocytes

Bacteriophage-encoded depolymerases: their diversity and biotechnological applications

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