ESTIMATION OF ELASTOLYTIC ACTIVITY OF STRAINS OF
            <i>PSEUDOMONAS AERUGINOSA</i>

Mull, John D.; Callahan, Walter S.

doi:10.1128/jb.85.5.1178-1179.1963

Cited by 14 publications

(4 citation statements)

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“…Recently, Mandl et al (1962) showed that some strains of P. aeruginosa can produce elastase, but other strains fail to show any elastolytic activity. A similar phenomenon was observed by Mull and Callahan (1963) and Oakley and Banerjee (1963). Nevertheless, my previous report (Morihara, 1962) showed that P. aeruginosa strains produce proteinase in a high yield regardless of their origin.…”

supporting

confidence: 78%

“…Recently, it was found (Mandl et al, 1962;Mull and Callahan, 1963;Oakley and Banerjee, 1963) that some strains of P. aeruginosa produce elastase but others do not. My data support this observation, and further show that the elastase-positive strains can produce proteinase in either synthetic or natural medium, in clear contrast to the elastase-negative strains which can produce proteinase only in synthetic medium containing Ca ion.…”

Section: Discussionmentioning

confidence: 99%

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PRODUCTION OF ELASTASE AND PROTEINASE BY PSEUDOMONAS AERUGINOSA

Morihara

1964

J Bacteriol

194

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Morihara, Kazuyuki (Shionogi Research Laboratory, Osaka, Japan). Production of elastase and proteinase by Pseudomonas aeruginosa . J. Bacteriol. 88: 745–757. 1964.—Some strains of Pseudomonas aeruginosa produced elastase, but the others did not. The elastase-positive strains produced two proteinases (fractions II and III), and the elastase-negative strains produced one proteinase (fraction III). Moreover, one proteinase (fraction I) was produced by both elastase-positive and elastase-negative strains, but the activity was small and negligible. The three proteinases were separated by column chromatography on diethylaminoethyl-cellulose, and elastolytic activity corresponded to fraction II. The effect of components of the medium was slight for production of fraction II; fraction III was produced only in synthetic medium containing Ca ion and not in natural medium. The optimal pH of fractions I, II, and III for casein was 6.5, 8.0, and 10.0, respectively; that of fraction II for elastin was 7.5 to 8.0. The other characters of the three proteinases also differed. Both the proteolytic and the elastolytic activities of fraction II showed a similar behavior for various treatments, except the inhibition test by NaCl and serum. Fraction III proteinases from various strains were identical in their enzymatic or other characters, showing that various strains were related regardless of the difference of their elastolytic activity. The reason that the elastolytic activity of P. aeruginosa differed according to the origin of the strain is discussed on the basis of a taxonomic study; results indicate that the ability to produce elastolytic activity (fraction II) may be a dissociative character of the species.

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supporting

confidence: 78%

Section: Discussionmentioning

confidence: 99%

PRODUCTION OF ELASTASE AND PROTEINASE BY PSEUDOMONAS AERUGINOSA

Morihara

1964

J Bacteriol

194

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“…The QS-induced expression of lasB and rhlA genes in P. aeruginosa encodes the production of elastase and rhamnolipids, respectively [ 37 , 38 , 39 ]. Elastase LasB, an extracellular zinc metalloprotease, facilitates extensive host colonization [ 40 ], suppresses the innate immune system [ 41 ] and causes damage to the host tissues [ 42 , 43 ] The elastase gene in P. aeruginosa was first discovered by Mandl and colleagues in 1962 [ 44 ] and later confirmed to be the major encoding gene for elastolytic activity responsible for the pathogenesis in P. aeruginosa -infected tissues [ 45 ]. This elastase enzyme has been identified as a possible therapeutic target to attenuate the mechanism of continuous virulence and progression of the disease by P. aeruginosa.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of the Quorum Sensing System, Elastase Production and Biofilm Formation in Pseudomonas aeruginosa by Psammaplin A and Bisaprasin

Oluwabusola¹,

Katermeran

Poh

et al. 2022

Molecules

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Natural products derived from marine sponges have exhibited bioactivity and, in some cases, serve as potent quorum sensing inhibitory agents that prevent biofilm formation and attenuate virulence factor expression by pathogenic microorganisms. In this study, the inhibitory activity of the psammaplin-type compounds, psammaplin A (1) and bisaprasin (2), isolated from the marine sponge, Aplysinellarhax, are evaluated in quorum sensing inhibitory assays based on the Pseudomonas aeruginosa PAO1 lasB-gfp(ASV) and rhlA-gfp(ASV) biosensor strains. The results indicate that psammaplin A (1) showed moderate inhibition on lasB-gfp expression, but significantly inhibited the QS-gene promoter, rhlA-gfp, with IC50 values at 14.02 μM and 4.99 μM, respectively. In contrast, bisaprasin (2) displayed significant florescence inhibition in both biosensors, PAO1 lasB-gfp and rhlA-gfp, with IC50 values at 3.53 μM and 2.41 μM, respectively. Preliminary analysis suggested the importance of the bromotyrosine and oxime functionalities for QSI activity in these molecules. In addition, psammaplin A and bisaprasin downregulated elastase expression as determined by the standard enzymatic elastase assay, although greater reduction in elastase production was observed with 1 at 50 μM and 100 μM. Furthermore, the study revealed that bisaprasin (2) reduced biofilm formation in P. aeruginosa.

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“…This is primarily owing to the lack of studies in which individually purified toxin preparations are used. Some of the agents known to be produced are a hemolysin (Liu, 1957;Berk, 1962), lecithinase (Esselmann and Liu, 1961), lipases (Muftic, 1954;Liu, Abe, and 13ates, 1961), protease (M\orihara, 1963), deoxyribonuclease (Streitfeld, Hoffmann, and Janklow, 1962), elastase (Mlandl, Keller, and Cohen, 1962;Mull and Callahan, 1963), muco-lytic enzyme (Bergamini, 1952), gelatinasefibrinolytic enzymes (Kourilsky and Richou, 1954), and a toxic extracellular slime (Liu et al, 1961;Eagon, 1962). Recent interest in the Pseudomonas hemolysin has been renewed, owing to the discovery of an intracellular hemolytic agent which appears sometime after elicitation of the extracellular hemolysin when cultures are grown on solid media (Berk, unpublished data).…”

mentioning

confidence: 99%

PARTIAL PURIFICATION OF THE EXTRACELLULAR HEMOLYSIN OF PSEUDOMONAS AERUGINOSA

Berk

1964

J Bacteriol

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Through a series of chemical fractionation steps, the extracellular hemolysin of Pseudomonas aeruginosa was purified 126-fold with a recovery of 49%. Hemolytic activity of crude preparations was irreversibly lost upon contact with anionic exchange materials such as diethylaminoethyl Sephadex or ECTEOLA-Cellulose, but traveled with the solvent front during passage through Sephadex G-200 and carboxymethyl Sephadex. The hemolysin was soluble in water and ethanol, and was partially extractable with ether, but not with trichlorotrifluoroethane (Freon). Although normal serum and serum albumin blocked hemolytic activity, it was unaffected by trypsin, deoxyribonuclease, or ribo

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ESTIMATION OF ELASTOLYTIC ACTIVITY OF STRAINS OF PSEUDOMONAS AERUGINOSA

Cited by 14 publications

References 0 publications

PRODUCTION OF ELASTASE AND PROTEINASE BY PSEUDOMONAS AERUGINOSA

PRODUCTION OF ELASTASE AND PROTEINASE BY PSEUDOMONAS AERUGINOSA

Inhibition of the Quorum Sensing System, Elastase Production and Biofilm Formation in Pseudomonas aeruginosa by Psammaplin A and Bisaprasin

PARTIAL PURIFICATION OF THE EXTRACELLULAR HEMOLYSIN OF PSEUDOMONAS AERUGINOSA

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