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PubMed1981

[Immunogenic properties of Clostridium perfringens type A anatheta-hemolysin].

Guinea-pigs were immunized with anatheta-hemolysin preparations adsorbed on aluminum hydroxide, as well as with the mixture of anatheta-hemolysin and type A Cl. perfringens toxoid, purified and concentrated. Anatheta hemolysin preparations were obtained with the use of homogeneous theta hemolysin, as well theta hemolysin of various purification degrees. As a result, antatheta hemolytic guinea-pig sera capable of neutralizing 2,000-8,000 HU of theta-hemolysin were obtained. Tests made to establish the degree of protection in the immunized guinea-pigs did not show that the animals immunized with the mixture of anatheta-hemolysin and type A Cl. perfringens toxoid, purified and concentrated, had any advantages in the degree of protection over the animals immunized with the toxoid alone. But there is no doubt that this component plays a positive role under the conditions of natural gas gangrene when the hemolytic action of Cl. perfringens toxin becomes considerably pronounced.

Animals↗
PubMed1983

Transport of hemolysin by Escherichia coli.

The hemolytic phenotype in Escherichia coli is determined by four genes. Two (hlyC and hlyA) determine the synthesis of a hemolytically active protein which is transported across the cytoplasmic membrane. The other two genes (hlyBa and hlyBb) encode two proteins which are located in the outer membrane and seem to form a specific transport system for hemolysin across the outer membrane. The primary product of gene hlyA is a protein (protein A) of 106,000 daltons which is nonhemolytic and which is not transported. No signal peptide can be recognized at its N-terminus. In the presence of the hlyC gene product (protein C), the 106,000-dalton protein is processed to the major proteolytic product of 58,000 daltons, which is hemolytically active and is transported across the cytoplasmic membrane. Several other proteolytic fragments of the 106,000-dalton protein are also generated. During the transport of the 58,000-dalton fragment (and possible other proteolytic fragments of hlyA gene product), the C protein remains in the cytoplasm. In the absence of hlyBa and hlyBb the entire hemolytic activity (mainly associated with the 58,000-dalton protein) is located in the periplasm: Studies on the location of hemolysin in hlyBa and hlyBb mutants suggest that the gene product of hlyBa (protein Ba) binds hemolysin and leads it through the outer membrane whereas the gene product of hlyBb (protein Bb) releases hemolysin from the outer membrane. This transport system is specific for E coli hemolysin. Other periplasmic enzymes of E coli and heterologous hemolysin (cereolysin) are not transported.

Base Sequence↗
PubMed1963

PRODUCTION AND NATURE OF LISTERIA MONOCYTOGENES HEMOLYSINS.

Njoku-Obi, Augustine N. (School of Veterinary Medicine, Tuskegee Institute, Ala.), Edward M. Jenkins, Jessie C. Njoku-Obi, Joanne Adams, and Verdell Covington. Production and nature of Listeria monocytogenes hemolysins. J. Bacteriol. 86:1-8. 1963.-Hemolysin produced by various strains of Listeria monocytogenes varied in quality and quantity, depending on medium, incubation temperature and time, and biological variations in the organisms. The hemolysin was inactivated by filtration (through Seitz, Selas, or sintered-glass filters), heat, oxygen, and formalin. Sodium thiosulfate reactivated hemolysin inactivated by filtration and oxygen. The hemolysin was protein in nature, migrating electrophoretically as a gamma-globulin, and highly antigenic in the rabbit. Although no toxicity was observed in intact mice injected with hemolysin, a possible leukocytolysis was noted with isolated mice peritoneal exudate cells. Due to the high antihemolytic activity of normal sera from various species, the possible use of an antilisteriolysin test in serological diagnosis is questioned.

Animals↗
PubMed1963

MECHANISM OF ACTION OF STAPHYLOCCAL ALPHA-HEMOLYSIN. II. ANALYSIS OF THE KINETIC CURVE AND INHIBITION BY SPECIFIC ANTIBODY.

Marucci, Americo A. (Upstate Medical Center, Syracuse, N.Y.). Mechanism of action of staphylococcal alpha-hemolysin. II. Analysis of the kinetic curve and inhibition by specific antibody. J. Bacteriol. 86:1189-1195. 1963.-At least two steps are necessary before the rabbit erythrocyte is lysed by staphylococcal alpha-hemolysin. The first step involves the reaction of alpha-hemolysin with the red cell. The second step, leading to the release of hemoglobin, is an intrinsic reaction of the damaged red cell and takes place without further participation of hemolysin. The speed of this intrinsic reaction is temperature-dependent. Erythrocytes taken from the same rabbit do not vary in their susceptibility to the alpha-hemolysin. From the results of the experiments described herein, a preliminary hypothesis on the mechanism of action of staphylococcal alpha-hemolysin is given.

Animals↗
PubMed1964

PURIFICATION OF THE SOLUBLE HEMOLYSINS OF LISTERIA MONOCYTOGENES.

Jenkins, E. M. (Tuskegee Institute, Tuskegee, Ala.), A. N. Njoku-Obi, and E. W. Adams. Purification of the soluble hemolysins of Listeria monocytogenes. J. Bacteriol. 88:418-424. 1964.-A method is described for obtaining relatively purified hemolysin preparations from both virulent and avirulent strains of Listeria monocytogenes. These hemolysins are protein in nature as shown by heat lability, nondialyzable properties, precipitation with trichloroacetic acid, and electrophoretic mobility. The hemolysins are antigenic in rabbits as shown by serum neutralization tests. The potency of the purified hemolysin was markedly increased by cysteine, sodium hydrosulfite, and a number of reducing agents. Many of the actions of the purified hemolysin seemed to parallel that of streptolysin O, and certain of these activities could be explained by the "thioldisulfide hypothesis."

Animals↗
PubMed1996

Cloning and detection of the hemolysin gene of Vibrio anguillarum.

A 5 kb DNA fragment encoding a hemolysin was cloned from the fish pathogenic bacterium Vibrio anguillarum using the cosmid vector charomid9-36. An open reading frame of the hemolysin gene (VAH1) was 2253 bp and corresponded to a protein of 751 amino acid residues. The deduced amino acid sequence of the VAH1 gene and the previously reported Vibrio cholerae EI Tor hemolysin, V. vulnificus cytolysin-hemolysin, Aeromonas hydrophila AHH1 hemolysin, and A. salmonicida ASH4 hemolysin showed a significant degree of sequence homology, and the overall amino acid identities were 57.3%, 25.8%, 46.2%, and 43.7%, respectively. DNA hybridization analysis under high-stringent conditions using VAH1 as a probe, demonstrated that VAH1 hybridized with 25 out of 28 strains of V. anguillarum including serotypes A to I, but did not hybridize with other species of Vibrio, A. hydrophila or A. salmonicida. The targeted DNA fragment of VAH1 was successfully amplified from V. anguillarum-infected fish tissues by PCR.

Amino Acid Sequence↗
PubMed1997

Some properties of nicked Vibrio vulnificus hemolysin.

Vibrio vulnificus, an opportunistic human pathogen, secretes the 50 kDa single-chain hemolysin. When incubated with an exocellular protease from this vibrio, the 50 kDa hemolysin was cleaved in some peptides joined with the disulfide bond(s); the 40 kDa fragment and the small fragment(s) undetectable in SDS-PAGE. The nicked hemolysin induced comparable hemolysis through the same process as that of the intact toxin. However, the nicked hemolysin was found to be more stable against inactivation due to autoaggregation, so that it formed a larger precipitation zone in the single radial immunodiffusion test using the antiserum against the intact hemolysin. These results suggest that V. vulnificus hemolysin is modified to be a more hydrophilic protein by nicking, while it is not accompanied by loss of the hemolytic activity.

Bacterial Proteins↗
PubMed1995

Isolation of mutant toxins of Vibrio parahaemolyticus hemolysin by in vitro mutagenesis.

Thermostable direct hemolysin produced by Vibrio parahaemolyticus is a major virulence factor of the organism. The hemolysin has a variety of biological activities such as lethality to mice, cytotoxicity to cultured cells, cardiotoxicity, and fluid accumulating activity in rabbit ileal loop test. In this study, we attempted to isolate less hemolytic mutant toxins of the thermostable direct hemolysin to use them for analysis of mode of action of the hemolysin. Six mutant toxins were obtained by in vitro mutagenesis of the cloned gene for the hemolysin. Characterization of the mutant toxins demonstrated that single amino acid substitutions at Gly62, Trp65, Thr67, Gly86, Glu116 and Glu138 resulted in a loss or lowering of the hemolytic activity. Two of the mutant toxins inhibited hemolysis by wild-type toxin on rabbit blood agar plates, while their hemolytic activity was below the detectable level. These mutant toxins would be useful for identifying the as yet unknown receptor for the hemolysin on the target cell membrane.

Bacterial Toxins↗
PubMed1995

Cloning and primary structure of a new hemolysin gene from Bacillus cereus.

A new hemolysin gene from Bacillus cereus VKM-B164 was cloned in Escherichia coli and sequenced. Deduced protein consists of 219 amino acids and has a molecular mass of 24.4 kDa. It has been concluded that the hemolysin, named 'hemolysin III', is distinct from the B. cereus hemolysins reported previously: cereolysin, sphingomyelinase, cereolysin AB, hemolysin II, and 'cereolysin-like' hemolysin (Honda, T., Shiba, A., Seo, S., Yamamoto, J., Matsuyama, J. and Miwatani, T. (1991) FEMS Microbiol. Lett. 79, 205-210).

Amino Acid Sequence↗
PubMed2006

Purification and sensitivity of Clostridium chauvoei hemolysin to various erythrocytes.

Using ammonium sulphate fractionation, the Clostridium chauvoei hemolysin was purified by cation exchange chromatography and sephacryl S-100 gel filtration. The molecular mass of the hemolysin, determined by SDS-PAGE was found to be approximately 27kDa. The activity of the hemolysin was determined in erythrocytes of various animals, with sensitivities observed in the order of cow, sheep, chicken, rabbit, rat, mouse, dog and horse. Temperature affected the sensitivity of erythrocytes to C. chauvoei hemolysin. These results may reflect distinct characteristics of the hemolytic activity of C. chauvoei hemolysin and that the hemolysin may be pore-forming.

Animals↗
PubMed1988

Enterohemolysin, a new type of hemolysin produced by some strains of enteropathogenic E. coli (EPEC).

42 Escherichia coli O26 strains which had been isolated at geographically different places and over a long time period were examined for hemolysin synthesis. 17 of these were found to be hemolysin-negative, nine strains were found to produce plasmid encoded alpha-hemolysin and 16 strains were shown to produce a phenotypically different hemolysin. This new type of hemolysin was called enterohemolysin and found to be genetically and immunologically non-related with the already described E. coli alpha-hemolysin. Enterohemolytic E. coli were not found in feces of 200 healthy infants under the age of two years. However, four E. coli O111 strains, one O121:H- and one O25:K5:H- strain, all from infants with diarrhoea were also enterohemolysin producers.

Animals↗
PubMed1980

Characteristics of the interaction of a treponemal hemolysin with rabbit erythrocytes.

The mechanism of action on rabbit red cells of Treponema hyodysenteriae hemolysin was studied using volume analysis and release of hemoglobin. While fixation of the hemolysin on the erythrocytes is temperature independent, it appears that hemolysis is temperature dependent. The kinetics of hemolysis proceed according to a sigmoid curve characterized by a prelytic lag. The duration of the prelytic lag varies inversely with the quantity of hemolysin but the rate and the maximum value of hemolysis are directly proportional to the quantity of hemolysin. The effect of sucrose and trypan blue on the hemolysin and the the red cells suggest that erythrocyte lysis is likely to be induced by the hemolysin in a way different from that known for other hemolytic agents.

Animals↗
PubMed2002

Geographical variation in the presence of genes encoding superantigenic exotoxins and beta-hemolysin among Staphylococcus aureus isolated from bovine mastitis in Europe and USA.

The object was to examine the geographical variation in the presence of superantigenic exotoxins and beta-hemolysin among epidemiologically independent Staphylococcus aureus isolates from bovine mastitis. A total of 462 S. aureus isolates from nine European countries and USA were examined for the presence of genes encoding staphylococcal enterotoxins A-E, and H, toxic shock toxin-1 (TSST-1), and beta-hemolysin, and 128 of these were examined for exfoliative toxins A and B. The detection was done by PCR. Phenotypic methods were used to confirm the PCR-results. None of the 128 isolates carried the genes for exfoliative toxin A or B. The total proportion of isolates in which superantigenic exotoxins were detected varied from 2% (one isolate) of the Danish isolates to 65% (32 isolates) of the Norwegian isolates. This marked and highly significant geographical variation was also present for the individual exotoxins. The genes encoding enterotoxin C, TSST-1, and enterotoxin D were the most common superantigens. The present and earlier studies demonstrate that the superantigenic exotoxins that were investigated in this study, do not play a role in the pathogenesis of bovine S. aureus mastitis. In contrast to the geographical variation among superantigenic exotoxins, 97% of the isolates were PCR-positive for and/or produced beta-hemolysin on 5% calf blood agar. Except for three isolates, the Norwegian isolates were PCR-negative, but positive on 5% calf blood agar. Sequence variation in the primer regions in the beta-hemolysin encoding gene of the Norwegian isolates is suggested, and should be investigated further. The consistent presence of beta-hemolysin suggests that this factor, or a co-existing gene correlated to beta-hemolysin, may be an active virulence factor in the pathogenesis of bovine S. aureus mastitis.

Animals↗
PubMed1993

The role of hemolysin(s) in the pathogenesis of Serpulina hyodysenteriae.

Serpulina (Treponema) hyodysenteriae, an anaerobic beta hemolytic spirochaete, is the etiologic agent of swine dysentery. Not much is known at present about the virulence factors of S. hyodysenteriae. However, the hemolysin production of this bacterium is generally accepted to be a virulence factor. To study the exact role of hemolysin production in the pathogenesis of swine dysentery, the gene encoding a hemolysin, tly, was cloned and its nucleotide sequence determined. After inactivation of this gene, the virulence of a tly-minus mutant in mice was tested. The mutant had reduced hemolysis indicating that the tly-encoded hemolysin was not the only hemolysin produced by S. hyodysenteriae. Mice infected with the tly-minus mutant had fewer cecal lesions than mice infected with the wild-type S. hyodysenteriae. It was concluded that the tly-encoded hemolysin might be an important virulence factor, but not the only one. Since it was demonstrated that spirochaetes can be transformed through electroporation, this has made a genetic approach to elucidate the pathogenesis of spirochaetal infections possible.

Animals↗
PubMed1993

Functional replacement of the hemolysin A transport signal by a different primary sequence.

Secretion of the 107-kDa hemolysin A (HlyA) from Escherichia coli is mediated by the membrane proteins hemolysin B and hemolysin D. Hemolysin B is a member of the so-called ATP binding cassette transporter superfamily, which includes the multidrug resistance P-glycoprotein, the cystic fibrosis CFTR protein, and the major histocompatibility complex-associated transporter of antigenic peptides. Recognition of HlyA by the hemolysin B/D transporter is dependent on a signal sequence mapped to the C-terminal 50 or so amino acids of the HlyA molecule. We show that the C-terminal 70 amino acids of leukotoxin from Pasteurella hemolytica can substitute functionally for the HlyA signal sequence. This 70-amino acid sequence contains no primary sequence similarity to the HlyA signal sequence; however, structural motifs of helix-turn-helix followed by strand-loop-strand can be deduced for both sequences. We also demonstrate by site-directed mutagenesis that changes to these predicted motifs affect transport function. It thus appears that the transport signal of HlyA may be defined by a higher-order structure and that the hemolysin transporter may recognize a much wider diversity of primary sequences than previously anticipated. This finding may have implications for understanding the basis of substrate specificity of other ATP binding cassette transporters.

Adenosine Triphosphate↗
PubMed1978

Behavior of a vigorous alpha- or beta-hemolysin-producing strain of Staphylococcus aureus in the cutaneous tissue of mice.

Two strains of Staphylococcus aureus were examined for behavior in the cutaneous tissue of mice by the fluorescent antibody technique, hematoxylin and eosin staining. When about 10(8) viable cells of an alpha-hemolysin-producing strain (Wood 46) were inoculated subcutaneously into a mouse, they multiplied in the subcutaneous tissue of the mouse and gradually entered the corium to produce alpha-hemolysin and nuclease. Edematous and necrotic lesions were observed in the cutaneous tissue where the organisms had multiplied. When 10(8) viable cells of a beta-hemolysin-producing strain (Kitami 3-9D) were inoculated into a mouse, they multiplied within a narrow extent surrounded mainly by infiltrating leukocytes and produced mainly beta-hemolysin. The changes of cutaneous tissue were weaker in mice inoculated with Kitami 3-9D strain than in mice inoculated with strain Wood 46. When 10(6) viable cells of both strains were inoculated into mice, they were phagocytized by leukocytes. Neither multiplication of organisms nor production of any active extracellular substance was observed in these mice. Edema, degeneration, and necrosis were also noticed in the cutaneous tissue of mice inoculated with alpha- and beta-hemolysin. In addition, the infiltration of leukocytes was inhibited mainly by alpha-hemolysin.

Animals↗
PubMed1997

Purification and characterisation of a hemolysin with phospholipase C activity from Vibrio cholerae O139.

A hemolysin was purified from a Vibrio cholerae O139 strain which moved as a single protein band of 67 kDa in SDS-PAGE. The hemolysin showed high level of phospholipase C activity. The purified phospholipase C-hemolysin demonstrated enterotoxic activity in rabbit ileal loop, suckling mice and enhanced permeability of rabbit skin. The pI of the purified hemolysin was 6.4. Erythrocytes from rabbit, chicken, guinea pig, sheep and horse were sensitive to the purified hemolysin in decreasing order of intensity. Erythrocytes from human and cow were unaffected by purified hemolysin.

Animals↗
PubMed1998

The erythrocyte receptor for Fusobacterium necrophorum hemolysin: phosphatidylcholine as a possible candidate.

An attempt was made to determine the receptor for the hemolysin of Fusobacterium necrophorum using horse erythrocyte or its membranes as target. The spectrum of erythrocyte sensitivity has indicated that horse, dog and mouse erythrocytes are highly sensitive whereas cattle, sheep, goat and chicken red blood cells are insensitive to this hemolysin. A high correlation between sensitivity and phosphatidylcholine content of the erythrocyte membranes was noted. Binding of hemolysin to horse erythrocyte membranes was reduced significantly by prior treatment of membranes with phospholipase A2 but not with phospholipase C. Pretreatment of erythrocyte membranes with pronase, proteinase K, trypsin or neuraminidase did not alter binding of hemolysin to the membranes, suggesting that protein or sialyl residues are not involved as receptors. Gas liquid chromatography analysis showed that the fatty acid profile from hydrolysis of bovine liver phosphatidylcholine by hemolysin and phospholipase A2 were similar. In conclusion, this report presents evidence that phosphatidylcholine may be acting as a possible receptor for the hemolysin of F. necrophorum.

Animals↗