Production and properties of haemolysins from clinical isolates of the Proteeae

Senior, B. W.

doi:10.1099/00222615-25-1-17

Cited by 28 publications

(20 citation statements)

References 11 publications

(17 reference statements)

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“…It cannot be excluded that both hemolysins occur at the same time in one strain and that their activities overlap. The non-a-hemolysin-like activity, present in P. penneri TGH 6927-0, is not masked and physiologically corresponds with the cell-bound hemolysin described by several authors in both P. mirabilis and P. vulgaris strains (Kotelko et al 1983;Senior and Hughes 1987). In accordance with data published by Swihart and Welch (1990) the presence of the commonly occurring HpmA hemolysin could be expected.…”

Section: Discussionsupporting

confidence: 88%

Cell-free and cell-bound hemolytic activities of Proteus penneri determined by different Hly determinants

Łukomski

Serwecińska²,

Różalski³

et al. 1991

Can. J. Microbiol.

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A collection of 45 Proteus penneri strains was characterized with respect to their hemolytic activity and representative cell-free or only cell-bound hemolysin possessing strains were chosen for further study. Extracellular Proteus penneri hemolysin, which was investigated earlier by hybridization, reacted with monospecific antiserum against alpha-hemolysin of Escherichia coli. In this paper we also show, using the colony hybridization technique, that the alpha-hemolysin-like determinant is widely distributed among Proteus penneri strains. Because one of the strains tested, which expressed a high activity of cell-bound hemolytic factor, did not carry such a Hly determinant, the presence of a second hemolysin is postulated. We cannot demonstrate any difference in hybridization patterns of alpha- and beta-hemolytic Proteus penneri strains and accumulation of the toxin molecule inside the cells was also not observed. The existence of another control mechanism, external to the hly operon, for hemolysin gene is suggested.

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Section: Discussionsupporting

confidence: 88%

Cell-free and cell-bound hemolytic activities of Proteus penneri determined by different Hly determinants

Łukomski

Serwecińska²,

Różalski³

et al. 1991

Can. J. Microbiol.

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“…Hemolysins identified in Proteus species include HlyA and HpmA. HlyA, an extracellular calcium-dependent poreforming cytotoxin (448,450), is produced by strains of P. pen-neri (330,360) and by 40% of P. vulgaris strains tested but not by P. mirabilis strains (192). The hly genes from P. vulgaris are homologous to the hly genes of E. coli (192) and represent the Morganella, E. coli, Proteus, and Pasteurella family of hemolysins (192,193,399,449).…”

Section: Damage To the Host And Acquisition Of Nutrientsmentioning

confidence: 99%

“…In addition to this hemolysin, P. vulgaris, P. penneri, and P. mirabilis strains produce an unrelated hemolysin known as HpmA, as identified by immunoblot and DNA-DNA hybridization. These 166-kDa hemolysins, or cell-associated hemolysins (177,192,196,197,360,449), are calcium-independent (177,196,360) pore-forming toxins that insert into target eukaryotic membranes, causing the efflux of Na ϩ ions and subsequent cell lysis (34). The production of HpmA is observed only in actively growing and replicating organisms in the presence of erythrocytes (297,299), with maximum production occurring during the late logarithmic phase in P. mirabilis strains (398).…”

Section: Damage To the Host And Acquisition Of Nutrientsmentioning

confidence: 99%

Complicated Catheter-Associated Urinary Tract Infections Due toEscherichia coliandProteus mirabilis

et al. 2008

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SUMMARY Catheter-associated urinary tract infections (CAUTIs) represent the most common type of nosocomial infection and are a major health concern due to the complications and frequent recurrence. These infections are often caused by Escherichia coli and Proteus mirabilis. Gram-negative bacterial species that cause CAUTIs express a number of virulence factors associated with adhesion, motility, biofilm formation, immunoavoidance, and nutrient acquisition as well as factors that cause damage to the host. These infections can be reduced by limiting catheter usage and ensuring that health care professionals correctly use closed-system Foley catheters. A number of novel approaches such as condom and suprapubic catheters, intermittent catheterization, new surfaces, catheters with antimicrobial agents, and probiotics have thus far met with limited success. While the diagnosis of symptomatic versus asymptomatic CAUTIs may be a contentious issue, it is generally agreed that once a catheterized patient is believed to have a symptomatic urinary tract infection, the catheter is removed if possible due to the high rate of relapse. Research focusing on the pathogenesis of CAUTIs will lead to a better understanding of the disease process and will subsequently lead to the development of new diagnosis, prevention, and treatment options.

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“…In P. mirabilis and P. vulgaris, hemolysins of the S. marcescens type (HpmA) and of the E. coli type (HlyA) [46,47] are found. The HpmA type is more common and is, for example, found in all 63 tested P. mirabilis strains and in 23 of 24 tested P. vulgaris strains isolated from various infections and normal faeces [48].…”

Section: Hpma and Hpmb Of Proteus Mirabilis And Proteus Vulgarismentioning

confidence: 99%

The Family of Serratia Type Pore Forming Toxins

Hertle

2005

CPPS

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The Serratia marcescens hemolysin represents the prototype of a growing family of pore forming toxins. The available bacterial genome sequences reveal Serratia hemolysin homologues in additional species. However, only S. marcescens hemolysin has been studied in great molecular detail. This family of toxins has nothing in common with the pore forming toxins of E. coli type (RTX toxins), the Staphylococcus aureus alpha-toxin or the thiol activated toxin of group A beta-hemolytic streptococci (Streptolysin O). Studies on erythrocytes, eukaryotic cells and artificial black lipid membranes, have shown that the mechanism of pore formation of ShlA is different form other pore forming toxins. The S. marcescens hemolysin proteins ShlB and ShlA, exhibit protein sequence homologues in Proteus mirabilis, Haemophilus ducreyi, Yersinia pestis, Yersinia enterocolitica, Edwardsiella tarda, Photorhabdus luminescens and Xylella fastidiosa . The family of Serratia type pore forming toxins show a unique secretory mechanism which has been described as a two partner secretion system (TPSS) or type V-secretion system. Not only Serratia type pore forming toxins are secreted via TPSS but also adhesins from Bordetella pertussis, Erwinia chrysanthemi and Haemophilus influenzae. The uniqueness of the Serratia family is underlined by the fact that activation of ShlA by ShlB strictly requires phosphatidylethanolamine as a cofactor. And, quite unusual, ShlA undergoes a conformational change during activation.

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Production and properties of haemolysins from clinical isolates of the Proteeae

Cited by 28 publications

References 11 publications

Cell-free and cell-bound hemolytic activities of Proteus penneri determined by different Hly determinants

Cell-free and cell-bound hemolytic activities of Proteus penneri determined by different Hly determinants

Complicated Catheter-Associated Urinary Tract Infections Due toEscherichia coliandProteus mirabilis

The Family of Serratia Type Pore Forming Toxins

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