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PubMed1990

Domains of Escherichia coli hemolysin (HlyA) involved in binding of calcium and erythrocyte membranes.

The primary structure of Escherichia coli hemolysin (HlyA) contains a 9-amino-acid sequence which is tandemly repeated 13 times near the C terminus and which is essential for hemolytic activity. Hemolysin also requires an unknown modification by an accessory protein, HlyC, for hemolytic activity. The role of calcium in the interaction of HlyA with erythrocytes was investigated by using recombinant strains which produced inactive hemolysins unmodified by HlyC or deleted of the repeat sequences. 45Ca2+ autoradiography of the recombinant hemolysins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred to nitrocellulose showed that full-length, active hemolysin bound calcium. The domain involved in binding calcium was identified as the tandemly repeated sequences, since the deletion derivative missing 11 of the 13 repeats did not bind calcium. Inactive hemolysin, unmodified by HlyC, contained the repeated sequences and bound calcium as efficiently as the active, full-length toxin. The binding of the inactive toxins to erythrocytes was investigated by immunoblotting saline-washed, toxin-treated cells with monoclonal antibodies after sodium dodecyl sulfate-polyacrylamide gel electrophoresis separation of membrane proteins. The binding of full-length, active hemolysin to erythrocytes was calcium dependent. Inactive hemolysin deleted of the repeat units did not bind to cells. The inactive hemolysin, unmodified by HlyC, bound calcium but did not bind to erythrocytes. These results highlight the importance of calcium in the binding of hemolysin to erythrocytes and suggest that the binding of hemolysin to cells requires an interaction between the calcium-binding repeat domain and the modification produced by the HlyC protein.

Animals↗

PubMed1980

Properties of a hemolysin produced by group B streptococci.

A hemolysin that appears to be responsible for the zones of beta-hemolysis surrounding colonies of group B streptococci (Streptococcus agalactiae) on blood agar plates has been isolated and partially purified. No soluble hemolysin was detectable in the supernatants of streptococcal cultures grown in several types of media. However, hemolytic activity was detected when streptococci were incubated with erythrocytes, and soluble hemolysin was isolated when bacterial suspensions were incubated in the presence of a variety of agents, including calf serum, albumin, Tween 80, and starch. Glucose and other fermentable carbohydrates stimulated hemolysin production, and metabolic inhibitors greatly reduced the titer of hemolysin that could be recovered, suggesting that cellular metabolism is necessary for hemolysin production or release. The soluble hemolysin was concentrated by ammonium sulfate precipitation and partially purified by gel filtration. Agents known to inhibit other streptococcal hemolysins, including phospholipids, trypan blue, proteases, and cholesterol, were tested for their effect on the group B hemolysin. Only the phospholipids inhibited hemolysin activity. The group B streptococcal hemolysin appears to be similar to, but distinct from, streptolysin S produced by Streptococcus pyogenes.

Blood↗

PubMed2001

Oxidized low-density lipoprotein-binding specificity of Asp-hemolysin from Aspergillus fumigatus.

Oxidized low-density lipoprotein (Ox-LDL) is known to be involved in the generation and progression of atherosclerosis. Ox-LDL has a number of potentially atherogenic effects on vascular cells, including the uncontrolled uptake by scavenger receptors. We have previously shown that Asp-hemolysin binds to Ox-LDL in a concentration-dependent manner. The present study was undertaken to clarify the binding specificity of Asp-hemolysin to Ox-LDL. We examined the binding specificity of Asp-hemolysin to Ox-LDL using several modified lipoproteins and scavenger receptor ligands. Asp-hemolysin bound to Ox-LDL with shorter LDL oxidation times. However, Asp-hemolysin did not bind to the acetylated LDL. The native high-density lipoprotein (n-HDL) and modified HDL (e.g., acetylated HDL, oxidized HDL) also had no Asp-hemolysin binding. Furthermore, inhibitors of the scavenger receptor binding, including maleylated BSA, polyinosinic acid, dextran sulfate and fucoidin, had no effect on the binding of Ox-LDL to Asp-hemolysin. Surface plasmon resonance studies revealed that Ox-LDL binds with high affinity (K(D)=0.63 microg/ml) to Asp-hemolysin. We concluded that Asp-hemolysin is a specific binding protein with a high affinity for Ox-LDL, and its binding specificity is distinct from any receptor for Ox-LDL. The present studies suggest that Asp-hemolysin may bind to Ox-LDL using a mechanism different from the scavenger receptors.

Aspergillus fumigatus↗

PubMed2000

Genetic and biochemical properties of a hemolysin (pyolysin) produced by a swine isolate of Arcanobacterium (Actinomyces) pyogenes.

Arcanobacterium (Actinomyces) pyogenes, a causative agent of various pyogenic diseases in domestic animals, produces a hemolysin which is thought to be an important virulence factor. This hemolysin was purified from the culture supernatant of A. pyogenes swine isolate. The purified hemolysin showed a single band with a molecular mass of 56 kDa on SDS-polyacrylamide gel electrophoresis, and its isoelectric point was 9.2. The activity of this hemolysin was not enhanced by the addition of L-cysteine or sodium thioglycolate, but it was inhibited by cholesterol. The gene encoding the hemolysin was cloned, sequenced and expressed in Escherichia coli by means of ZAP Express vector. Analysis by SDS-polyacrylamide gel electrophoresis with immunoblotting showed that the molecular weight of the hemolysin expressed in E. coli is the same as that of the hemolysin purified from A. pyogenes. Nucleotide sequence analysis revealed an open reading frame of 1,605 bp encoding a 534 amino acid protein of 57,989 Da. The nucleotide sequence of the hemolysin gene from A. pyogenes swine isolate differed only slightly (97.6% identity) from the sequence of plo gene from A. pyogenes strain BBR1 reported by Billington et al (J. Bacteriol. 179: 6100-6106, 1997). The cysteine residue existed in the undecapeptide region of the hemolysin, which is highly conserved in thiol-activated cytolysins (cholesterol-binding cytolysins), and is replaced with alanine. Therefore, the hemolysin of A. pyogenes seems to be a novel member of the thiol-activated cytolysin family.

Actinomycetaceae↗

PubMed1981

Membrane-damaging and cytotoxic effects on human fibroblasts of alpha- and beta-hemolysins from Aeromonas hydrophila.

The effects of two hemolysins (alpha and beta) from Aeromonas hydrophila on human lung fibroblasts were investigated. The toxins differed distinctly in regard to the morphological changes they produced. The alpha-hemolysin caused rounding of the cells. The beta-hemolysin caused a striking vacuolization of the cytoplasm in cells which remained spread out on the growth surface. The toxins also differed as to relative size of the initial lesions they induced in the fibroblast membrane, scored by leakage of different-sized cytoplasmic markers. The alpha-hemolysin induced larger lesions than did the beta-hemolysin. It was indirectly demonstrated that the alpha-hemolysin did not bind, or bound only transiently, to the fibroblasts. By contrast, the beta-hemolysin bound rapidly and firmly. The cytopathogenic response to the alpha-hemolysin was reversible, whereas cells treated with small amounts of the beta-hemolysin for only 1 min invariably died within a few hours. Thus, the two hemolysins from A. hydrophila, despite many biochemical similarities, show essential dissimilarities in their interactions with cultured cells.

Aeromonas↗

PubMed1971

Cross-neutralization of leptospiral hemolysins from different serotypes.

Cross-neutralization studies on leptospiral hemolysins from strains of two antigenically different serotypes, pomona and canicola, were conducted in sheep. A third strain of serotype hardjo that does not produce hemolysin and is antigenically distinct was included for control purposes. Concentrated hemolysins, prepared from supernatant fluids of canicola or pomona cultures, produced hemolytic anemia in sheep after intravenous injection. Sheep previously infected with hemolysin-producing strains were refractory to effects of homologous or heterologous hemolysins. On the other hand, infection with hardjo did not confer immunity to the action of hemolysins. Hemolysin-neutralizing antibodies were demonstrable in sheep previously infected with pomona or canicola only after challenge with homologous or heterologous hemolysins. Cross-neutralization between two hemolysins were demonstrable in vitro. Hemolysin-neutralizing antibody titers did not correlate with agglutinin titers. Concentrated supernatant fluid of the hardjo culture provoked toxic reactions predominantly in sheep previously infected with pomona or canicola. The causes of these untoward reactions were not determined.

Albuminuria↗

PubMed1999

Prevalence of, antibody response to, and immunity induced by Haemophilus ducreyi hemolysin.

Haemophilus ducreyi, the etiologic agent of chancroid, a genital ulcer disease, produces a cell-associated hemolysin whose role in virulence is not well defined. Hemolysin is encoded by two genes, hhdA and hhdB, which, based on their homology to Serratia marcescens shlA and shlB genes, are believed to encode the hemolysin structural protein and a protein required for secretion and modification of this protein, respectively. In this study, we determined the prevalence and expression of the hemolysin genes in 90 H. ducreyi isolates obtained from diverse geographic locations from 1952 to 1996 and found that all strains contained DNA homologous to the hhdB and hhdA genes. In addition, all strains expressed a hemolytic activity. We also determined that hemolysin is expressed in vivo and is immunogenic, as indicated by the induction of antibodies to hemolysin in both the primate and rabbit disease models as well as in human patients with naturally acquired chancroid. Wild-type strain 35000 and isogenic hemolysin-negative mutants showed no difference in lesion development in the temperature-dependent rabbit model. However, immunization of rabbits with the purified hemolysin protein reduced the recovery of wild-type H. ducreyi, but not hemolysin-negative mutants, from lesions. Our study indicates that hemolysin is a possible candidate for vaccine development due to its immunogenicity, expression in vitro and in vivo by most, if not all, strains, and the effect of immunization on reducing the recovery of viable H. ducreyi in experimental disease in rabbits.

Animals↗

PubMed1980

Synthesis and secretion of hemolysin by Escherichia coli.

Hemolytic Escherichia coli cells were found to synthesize and secrete significant amounts of hemolysin into a mineral salt-glucose medium containing hemoglobin. The release of de novo-synthesized hemolysin was stopped in the presence of energy metabolism inhibitors such as 2,4-dinitrophenol, sodium azide, or potassium cyanide, resulting in an accumulation of intracellular hemolysin. A similar effect was observed in the presence of procaine, a neuroactive drug which inhibits the processing of exoproteins. Small amounts of hemolysin were secreted into the medium within approximately 10 min of inhibition of protein synthesis by chloramphenicol. This represented the final release of preformed periplasmic hemolysin en route to secretion through the outer membrane and was not caused by adsorption of external hemolysin to the cell surface. This secretion was not energy dependent but was inhibited above pH 8 and at low temperatures (10 to 20 degrees C). We concluded that two transport processes are involved in hemolysin secretion. De novo-synthesized hemolysin is extruded by an energy-dependent process through the cytoplasmic membrane and probably requires processing. In the periplasmic space a small internal pool of preformed hemolysin is accumulated temporarily before being transported through the outer membrane. Release of hemolysin through the outer membrane does not require energy or de novo protein synthesis.

Azides↗

PubMed1966

Production and characteristics of hemolysins of Escherichia coli.

Snyder, Irvin S. (University of Iowa, Iowa City), and Nancy A. Koch. Production and characteristics of hemolysins of Escherichia coli. J. Bacteriol. 91:763-767. 1996.-Filterable and nonfilterable hemolysins were produced by Escherichia coli in beef-heart infusion, casein hydrolysate, and chemically defined media. Differences were found among the three media in the time of appearance and in the relationship between production of these two hemolysins. The nonfilterable hemolysin produced in the three media, as well as the filterable hemolysin produced in the beef-heart infusion medium, were destroyed in 1 hr at 56 C. The filterable hemolysin produced in the casein hydrolysate and chemically defined media was unaffected by exposure to 56 C for 1 hr. Formalin inactivated the hemolysins produced in all three media. The optimal pH for activity of the nonfilterable hemolysin varied with time of production, whereas the optimal pH for the filterable hemolysin was constant. Certain carbohydrates were required for the production of filterable hemolysin by E. coli grown in casein hydrolysate and chemically defined media.

Caseins↗

PubMed2001

[Interactions between Asp-hemolysin from Aspergillus fumigatus and blood plasma components].

Asp-hemolysin is a cytolytic toxin that is produced by Aspergillus fumigatus. This toxin is lytic for erythrocytes of humans, rabbits and sheep. However, Asp-hemolysin is inactivated by the addition of serum or blood plasma. This study was undertaken to identify plasma components inhibitory to the hemolytic activity of Asp-hemolysin. alpha 2-Macroglobulin (alpha 2M) was isolated from the human blood plasma by affinity chromatography on a column containing Asp-hemolysin coupled to Sepharose. However, the hemolytic activity was only partially inhibited by alpha 2M. Apolipoprotein B (apoB)-containing lipoproteins, such as low density lipoprotein (LDL), inhibit the activity of this hemolytic toxin. When 20 micrograms apoB was added, the hemolytic activity was almost completely inhibited. Furthermore, similar inhibition was observed in the filtrates separated from the incubation mixture of Asp-hemolysin with LDL or apoB following ultrafiltration through a membrane with a molecular mass cutoff of 100,000. These results suggest that the inhibition by LDL is due to apoB binding to Asp-hemolysin. The binding activity of LDL to Asp-hemolysin was measured. LDL binds to Asp-hemolysin with an affinity as high as the LDL receptor. The apparent Kd, determined by Scatchard plot analysis, was 8.9 x 10(-9) M 125I-LDL. Oxidized LDL (Ox-LDL), but not acetylated LDL, inhibited the hemolytic activity of this toxin. The inhibitory effects of Ox-LDL increased with the time of Cu(2+)-induced LDL oxidation. Similar inhibition was observed in the filtrate separated from the incubation mixture of Asp-hemolysin with Ox-LDL (for 2 h of oxidation) following ultrafiltration through a membrane with a molecular mass cutoff of 100,000. However, at longer LDL oxidation times, the inhibition by the filtrates was less than the control mixture without ultrafiltration. These results suggest that the inhibition of the hemolytic activity by Ox-LDL was due to the binding of Ox-LDL to Asp-hemolysin at short LDL oxidation times.

Animals↗

PubMed1990

[Relationship between the anti-hemolysin activity and the structure of catechins and theaflavins].

We examined the corresponding isomers of catechins and theaflavins for anti-hemolysin activities against Staphylococcus aureus alpha-toxin and Vibrio cholerae O1 hemolysin. Catechins and theaflavins showed anti-hemolysin activities in a dose-dependent manner. Among the catechins tested, (-)catechin gallate, (-)epicatechin gallate and (-)epigallocatechin gallate having galloyl groups in their molecules showed more potent anti-hemolysin activities against both toxins. On the other hand, free catechins, i. e. (-)catechin, (-)gallocatechin, (-) epicatechin and (-)epigallocatechin had low anti-hemolysin activities against alpha-toxin. Although (-)catechin or (-)gallocatechin had no effect on cholera hemolysin, (-) epicatechin and (-)epigallocatechin were slightly inhibitory. Among dextrocatechins, (+) epicatechin and (+)epigallocatechin proved to be more effective than (+)catechin and (+) gallocatechin. The anti-hemolysin activities of theaflavins against alpha-toxin and cholera hemolysin were dependent on the number of the galloyl group in their structure. These results suggest that the tertiary structure of the catechin or theaflavin and the active site of hemolysin, that affects the interaction between them, plays an important role in the anti-hemolysin activity.

Biflavonoids↗

PubMed1992

Production, purification, and characterization of botulinolysin, a thiol-activated hemolysin of Clostridium botulinum.

A hemolysin, botulinolysin, produced by Clostridium botulinum was purified to homogeneity and characterized. First, a strain of C. botulinum type C, strain C-203 Tox, which produced a large amount of hemolysin, was selected, and optimal culture medium and conditions for its production of hemolysin were determined. The hemolysin produced in the culture supernatant of this strain under optimal conditions was purified by a combination of ammonium sulfate precipitation, DEAE-Sepharose CL-6B column chromatography, Sephadex G-75 gel permeation chromatography, and SP-Toyopearl 650 M cation-exchange column chromatography, with a recovery of 12%. The purified hemolysin gave a single protein band in polyacrylamide gel electrophoresis (PAGE) with and without sodium dodecyl sulfate (SDS). The protein in this band in PAGE with SDS was estimated to have a molecular weight of 58,000 and was immunostained with a neutralizing monoclonal antibody. In PAGE without SDS, the hemolytic activity corresponded in position to the single protein band. The pI of the hemolysin was 8.4. Amino acid analysis of the purified hemolysin indicated the presence of four half-cystine residues per molecule. The purified hemolysin had a specific activity of 2,100 hemolytic units per microgram of protein on rabbit erythrocytes. It was activated by SH compounds, inhibited by cholesterol, and heat labile. The optimum pH for hemolysis was 6.0 to 7.0. Rabbit, human, and guinea pig erythrocytes were the most susceptible to the hemolysin, while sheep, mouse, rat, and chicken erythrocytes were much less susceptible. The purified hemolysin had a lethal effect in mice and was cytotoxic for some cultured cells: its 50% lethal dose in mice was 310 ng, and its 50% cytotoxic dose for Vero cells was 120 ng/ml.

Amino Acids↗

PubMed1994

Hemolysin II is more characteristic of Bacillus thuringiensis than Bacillus cereus.

To investigate the distribution of the hemolysin II determinant among strains of Bacillus cereus and Bacillus thuringiensis, thirteen strains of B. cereus and fourteen strains of B. thuringiensis strains were tested for hybridization of their chromosomal DNAs with a DNA probe containing the B. cereus hemolysin II gene. In addition, the production of hemolysin II, whose activity is not inhibited by cholesterol, was tested. The presence (absence) of the hydridization response in the microorganisms's genome correlated with the presence (absence) of cholesterol-unaffected hemolysin production. Only four out of thirteen B. cereus strains were found to give a positive response in hybridization experiments, whereas thirteen out of fourteen B. thuringiensis strains responded positively. DNAs from ten B. thuringiensis strains contained a 3.5 kb EcoRV fragment, which hybridized with the B. cereus hemolysin II gene probe. The 3.5 kb EcoRV DNA fragment from one of these strains (B. thuringiensis VKM-B1555) was cloned and expressed in Escherichia coli cells. The hemolysin encoded by the cloned DNA fragment was not inhibited by cholesterol and possessed all other properties of B. cereus hemolysin II. The obtained data clearly show limited distribution of hemolysin II among B. cereus strains and demonstrate that hemolysin II is more characteristic of B. thuringiensis than B. cereus.

Bacillus cereus↗

PubMed1997

Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle.

Vibrio cholerae hemolysin is an extracellular pore-forming monomeric protein with a native molecular weight of about 60,000. In this study, we showed that the hemolysin interacted with immobilized phospholipids and cholesterol and formed oligomers in vesicles constituted from phospholipids alone with a stoichiometry identical to those produced in rabbit erythrocyte membrane. However, the hemolysin bound to glycoproteins with terminal beta1-galactosyl residues and an association constant of 9.4 x 10(7) M(-1) was estimated for the hemolysin-asialofetuin complex by solid phase binding assay. Oligomerization of the hemolysin in lipid bilayer converted the sugar-binding monomer to a lectin with strong carbohydrate-dependent hemagglutinating activity accompanied by inactivation of hemolytic activity and loss in ability to interact with phospholipids. There was no evidence for erythrocyte surface carbohydrates playing an essential role in interaction of the hemolysin with the cell. However, specific glycoproteins inhibited hemolysis of rabbit erythrocytes as well as interaction of the hemolysin with phospholipid. The results suggest (i) V. cholerae hemolysin is a monomer with distinct domains associated with specific binding to carbohydrates and interaction with lipids, (ii) the pore-forming property depends solely on the protein-lipid interaction with no evidence for involvement of sugars, and (iii) specific sugars can down-regulate the ability of the hemolysin to form pores in lipid bilayers.

Animals↗

PubMed1996

Pore-forming properties of the plasmid-encoded hemolysin of enterohemorrhagic Escherichia coli O157:H7.

Lipid bilayer experiments were performed with the plasmid-encoded hemolysin of enterohemorrhagic Escherichia coli (EHEC) O157:H7 strain EDL933. EHEC-hemolysin caused the formation of transient ion-permeable channels by integration in lipid bilayer membranes composed of asolectin, dioleoylglycerophosphoethanolamine and phosphoserine but not of diphytanoylglycerophosphocholine. Channel formation showed the same characteristics when culture supernatants of E. coli strains EDL 933 or HB101/pEO40, precipitated or purified EHEC-hemolysin were used for these experiments. The EHEC-hemolysin channels had two different states at small transmembrane potential (20 mV): a prestate that represented the first step of channel formation (single-channel conductance 40 pS in 0.15 M KCl) and an open state (550 pS in 0.15 M KCl at pH 6.0). Experiments with different salts suggested that the EHEC-hemolysin-induced channels were cation-selective at neutral pH. The mobility sequence of the cations within the channels resembles their mobility sequence in the aqueous phase. The single-channel data were consistent with the formation of wide, water-filled channels by the EHEC hemolysin. The single channel conductance was strongly pH dependent and increased over 2.5-fold in the pH range 5-8. The analysis of the single-channel data using the Renkin correction factor suggested that the EHEC-hemolysin formed channels with an average diameter of 2.6 nm. This size could be confirmed by the results of osmotic-protection experiments. Neither sucrose nor raffinose inhibited toxin-dependent hemolysis, whereas hemolysis did not occur in the presence of dextran 4 (molecular mass, 4 kDa). Our results demonstrate that EHEC-hemolysin can be considered to be a highly active repeats-in-toxin (RTX)-toxin with a similar but not identical pore-forming capacity as the chromosomal encoded E. coli alpha-hemolysin.

Electric Conductivity↗

PubMed1999

Hybridization analysis of the gene encoding a hemolysin (suilysin) of Streptococcus suis type 2: evidence for the absence of the gene in some isolates.

A hemolysin gene was cloned from a virulent strain of Streptococcus suis type 2 strain 1933. Analysis of the gene and its product revealed that it is identical to a previously reported hemolysin (suilysin) of S. suis type 2. Southern hybridization analysis of the digested total genomic DNA from S. suis with the cloned hemolysin DNA sequences as probe indicated that the hemolysin gene is present as a single copy on the genome. Genomic DNA of 63 isolates of S. suis encompassing all known serotypes were examined by DNA hybridization and polymerase chain reaction (PCR) studies for the presence of the hemolysin gene homolog. The results of both techniques were identical and demonstrated the absence of the hemolysin gene in some isolates. In DNA hybridization studies, three DNA probes derived from the hemolysin encoding gene were used. Results showed that sequences encoding the C-terminal 257 amino acid residues (Probe 1) were the most conserved and hybridized to a 1.2 kb fragment in 32 (51%) strains and a 4.0 kb fragment in 23 (36%) strains respectively. Thus, Probe 2 hybridized to the DNA of 55 (87%) of the isolates tested. The first probe (Probe 1) comprising almost the entire hemolysin gene and the third probe (Probe 3) which consisted of the N-terminal sequences hybridized only to a 4.0 kb fragment in 23 (36%) of the strains tested. Eight (13%) of the strains tested were hybridization and PCR negative. The hybridization of the C-terminal end sequences (Probe 2) to the 1.2 kb fragment in 32 (51%) of the strains and the lack of hybridization of the probes to eight (13%) strains may suggest the presence of different types of hemolysin molecule in S. suis strains.

Animals↗

PubMed2005

Identification and classification of all potential hemolysin encoding genes and their products from Leptospira interrogans serogroup Icterohae-morrhagiae serovar Lai.

AIM: To identify and classify all potential hemolysin candidates of Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai. METHODS: All of the potential hemolysin encoding genes were characterized in silico. These genes were cloned and expressed in Escherichia coli. The hemolytic activities of the expressed proteins were assayed observing the hemolysis on sheep blood agar plates. Sphingomyelinase activities of the hemolysin candidates were measured by thin-layer chromatography (TLC) and HPLC for sphingomyelin-hydrolysis. Expression and secretion of the hemolysins in L interrogans were studied by reverse transcription polymerase chain reaction, Western blot, and enzyme-linked immunosorbent assays. RESULTS AND CONCLUSION: The hemolytic activities of hemolysin candidates (LA0327, LA0378, LA1027, LA1029, LA1650, LA3050, LA3937, LA4004) from L interrogans strain Lai were confirmed. They were further divided into two groups, sphingomyelinase hemolysins and non-sphingomyelinase hemolysins, based on their ability to hydrolyze sphingomyelin. Most of these hemolysins were actually expressed in living L interrogans and some of them were secreted into the environment. This study establishes an essential and complete basis for further studying the contribution of hemolysins to the pathogenesis of L interrogans.

Amino Acid Sequence↗

PubMed1978

Purification and characterization of an immunologically distinct delta-hemolysin from a canine strain of Staphylococcus aureus.

Culture supernatants of 26 strains of Staphylococcus aureus possessing delta-hemolytic activity have been tested by immunodiffusion against a serum raised against purified delta-hemolysin from S. aureus CN 4108 (Newman D2). Supernatants from 14 strains of canine origin gave a reaction of partial identity with delta-hemolysin from CN 4108, whereas supernatants from all other strains had full identity. Delta hemolysin from one of these canine strains, CN 7450, was purified by ammonium sulfate fractionation and precipitation at pH 4.5. The physical, chemical, and biological properties of this toxin were compared with those of delta-hemolysin from CN 4108. Differences in molecular weight (as judged by Sepharose 6B chromatography), isoelectric point, and amino acid composition were found. Both toxins caused dermonecrosis in rabbits, lysed erythrocytes from several different species, and were inhibited by normal sera and phospholipids. Unlike delta-hemolysin from CN 4108, the hemolytic activity of delta-hemolysin from CN 7450 was found to be dependent on the incubation temperature over the range of 25 to 37 degrees C. Immunodiffusion results obtained with antisera raised against purified delta-hemolysin from CN 7450 indicated that delta-hemolysins from the canine strains were probably identical and confirmed that these differ immunologically from delta-hemolysin from CN 4108.

Amino Acids↗