Elastase of
            <i>Pseudomonas aeruginosa</i>
            : Inactivation of Complement Components and Complement-Derived Chemotactic and Phagocytic Factors

Schultz, Duane R.; Miller, Kent D.

doi:10.1128/iai.10.1.128-135.1974

Cited by 180 publications

(51 citation statements)

References 19 publications

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“…Similar characteristics for generation of chemotactic activity in serum, as we here describe for B. gingivalis, have previously been found for Streptoeoeeus pyogenes and Pseudomonas aeruginosa (15,19,29,30,31). Streptoeoeeus pyogenes has a surface bound C5a peptidase that specifically removes a six-aminoacid fragment from the C terminus of human C5a and abrogates the activity of the chemotaxin (15,30).…”

Section: Discussionsupporting

confidence: 82%

Generation and degradation of the complement fragment C5a in human serum by Bacteroides gingivalis

Sundqvist¹,

Bengtson²,

Carlsson³

1988

Oral Microbiology and Immunology

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The ability of Bacteroides gingivalis to generate chemotactic activity and the complement fragment C5a in human serum was assayed. When fresh serum was incubated with B. gingivalis there was a rapid increase of chemotactic activity of the serum during the first 15 min, but longer incubation resulted in loss of chemotactic activity. When heat‐inactivated serum was incubated with B. gingivalis similar increase and decrease of the chemotactic activity of serum was also observed. The chemotactic peptide C5a could be demonstrated in all sera showing chemotactic activity. The generation of C5a and possibly also other chemotactic substances in heat‐inactivated serum by B. gingivalis may mean that this chemotactic activity was formed from serum proteins by the proteolytic activity of B. gingivalis. The proteolytic activity of B. gingivalis may also be responsible for the inactivation of C5a generated in serum.

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Section: Discussionsupporting

confidence: 82%

Generation and degradation of the complement fragment C5a in human serum by Bacteroides gingivalis

Sundqvist¹,

Bengtson²,

Carlsson³

1988

Oral Microbiology and Immunology

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“…Following its purification and characterization by Morihara ef ai (1965), Pseudomonas elastase has been studied for both its proteolytic and elastolytic properties. Proteolytic effects of elastase include cleavage of immunoglobulln G proteins (Doring et ai, 1981), inactivation of alpha 1-proteinase inhibitor (Morihara ef ai, 1979), destruction of complement factors (Schultz and Miller, 1974), cleavage of human Received 6 August, 1991: revised 10 January, 1992accepted 16 January, 1991, 'Forcorrespondence, Tel, (614) 292 3761; Fax (614) 292 1538, type tl and IV collagens (Heck et ai. 1986b), and inactivation of human airway lysozyme (Jacquot ef ai.…”

Section: Introductionmentioning

confidence: 99%

Further studies on Pseudomonas aeruginosa LasA: analysis of specificity

Peters

Park

Darzins

et al. 1992

Molecular Microbiology

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Full elastolytic activity in Pseudomonas aeruginosa is a result of the combined activities of elastase, alkaline proteinase, and the lasA gene product, LasA. The results of this study demonstrate that an active fragment of the LasA protein which is isolated from the culture supernatant fraction is capable of degrading elastin in the absence of elastase, thus showing that LasA is a second elastase produced by this organism. In addition, it is shown that LasA-mediated enhancement of elastolysis results from the separate activities of LasA and elastase upon elastin. The LasA protein does not affect the secretion or activation of a proelastase as previously proposed in other studies. Furthermore, LasA has specific proteolytic capability, as demonstrated by its ability to cleave beta-casein. Preliminary analysis of beta-casein cleavage in the presence of various protease inhibitors suggests that LasA may be classified as a modified serine protease.

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“…A similar observation in a model of corneal infection with P aeruginosa in rats was obtained by Matsumoto et al (20). Further, it has also been reported that pseudomonal elastase destroys a wide range of substances of the host used for defense, such as immunoglobulin A (8), complement (28), and a plasma serine protease inhibitor (26), and that it suppresses neutrophil function (15).…”

Section: Discussionmentioning

confidence: 99%

Bradykinin Generation Triggered by Pseudomonas Proteases Facilitates Invasion of the Systemic Circulation by Pseudomonas aeruginosa

Sakata

Akaike

Suga

et al. 1996

Microbiology and Immunology

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To elucidate the mechanism of bacterial exoprotease in promotion of the intravascular dissemination of Pseudomonas aeruginosa, we examined the possible involvement of bradykinin (whose generation is induced by pseudomonal proteases in septic foci) in the invasion by bacteria, and in access of bacterial toxins to systemic blood circulation. P. aeruginosa 621 (PA 621), which produces very little protease, was injected intraperitoneally into mice together with pseudomonal exoproteases (elastase/alkaline protease). Dissemination of bacteria from the peritoneal septic foci to the blood was assessed by counting viable bacteria in the blood and spleen by use of the colony-forming assay. The results showed that pseudomonal proteases markedly enhanced (10-to 100-fold) intravascular dissemination of bacteria in mice. This enhancement was induced not only by pseudomonal proteases but also by bradykinin. More importantly, the increased spread of PA 621 induced by pseudomonal protease and bradykinin was significantly augmented by the addition of kininase inhibitors, indicating the direct involvement of bradykinin in bacterial dissemination. Similarly, bradykinin caused effective dissemination of pseudomonal toxins such as endotoxin (lipopolysaccharide) and exotoxin A when the toxins were injected into the peritoneal cavity with bradykinin. Furthermore, the lethality of the infection with PA 621 was strongly enhanced by pseudomonal proteases given i.p. simultaneously with PA 621. On the basis of these results, it is strongly suggested that pseudomonal proteases as well as bradykinin generated in infectious foci are involved in facilitation of bacterial dissemination in vivo.

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Elastase of Pseudomonas aeruginosa : Inactivation of Complement Components and Complement-Derived Chemotactic and Phagocytic Factors

Cited by 180 publications

References 19 publications

Generation and degradation of the complement fragment C5a in human serum by Bacteroides gingivalis

Generation and degradation of the complement fragment C5a in human serum by Bacteroides gingivalis

Further studies on Pseudomonas aeruginosa LasA: analysis of specificity

Bradykinin Generation Triggered by Pseudomonas Proteases Facilitates Invasion of the Systemic Circulation by Pseudomonas aeruginosa

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