PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Hemolysin Factors”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1983

[Relationship between hemolysin and hemolysin-destructive factor activities in Vibrio cholerae of Eltor biovar].

The study of hemolysin activity, hemolysin-destructive factor (HDF) activity and cholerogenicity in 143 Vibrio eltor strains has revealed the existance of close relationship between cholerogenicity and hemolysin production, as well as between cholerogenicity and HDF activity. The negative character of conjugation between the HDF activity and the hemolytic activity of the strains under study has been established, which allows one to suggest the possibility of the regulating action of hemolysin on the synthesis of HDF (enterotoxin).

Animals↗
PubMed1988

Purification of Chironex fleckeri venom components using Chironex immunoaffinity chromatography.

A comparison of the purification of the nematocyst venom of Chironex fleckeri by affinity immunochromatography using 13 different monoclonal antibodies was made. Varying degrees of purification of mouse lethal factor, hemolysin and dermonecrotic factors, as well as antigen positive proteins were achieved with each of the monoclonal antibodies. Although the protein curves of the chromatography were similar, each of the monoclonal antibody columns had a distinctive pharmacological and SDS-PAGE profile. At least two hemolysins (120,000 and 70,000 molecular weight), two dermonecrotic principles (120,000, less than 120,000) and three lethal factors (120,000, 70,000 and 14,500 molecular weight) were detected. The degree to which aggregation and fragmentation affects the molecular weights of these proteins is not known. It appears that multiple pharmacological activities are present within the same molecule since it is only with great difficulty that a pharmacological activity can be assigned to a specific molecular weight.

Animals↗
PubMed1989

Molecular epidemiology of adhesin and hemolysin virulence factors among uropathogenic Escherichia coli.

The pap, prs, pil, and hly operons of the pyelonephritic Escherichia coli isolate J96 code for the expression of P, F, and type 1 adhesins and the production of hemolysin, respectively; the afaI operon of the pyelonephritic E. coli KS52 encodes an X adhesin. Using different segments of these operons as probes, colony hybridizations were performed on 97 E. coli urinary tract and 40 fecal clinical isolates to determine (i) the presence in the infecting bacteria of nucleotide sequences related to virulence operons, and (ii) the phenotypic properties associated with such sequences. Coexpression of P and F adhesins encoded by pap-related sequences was detected more frequently among isolates from patients with pyelonephritis (32 of 49, 65%) than among those with cystitis (11 of 48, 23%; P less than 0.0001) or from fecal specimens (6 of 40, 15%; P less than 0.0001). Therefore, the expression of both adhesins appears to be critical in the colonization of the upper urinary tract. In contrast, afaI-related sequences were detected significantly more frequently among isolates from patients with cystitis, suggesting that this class of X adhesin may have a role in lower urinary tract infections. Urinary tract isolates differed from fecal isolates by a low incidence of type 1 adhesin expression among pil probe-positive isolates. hly-related sequences were only detected in pap probe-positive isolates. The frequency of hemolysin production among pap probe-positive isolates was not associated with a particular pattern of infection. The distribution of these virulence factors was similar in the presence or absence of reflux, indicating that structural abnormalities of the urinary tract did not facilitate colonization by adhesin-negative isolates.

Adhesins, Escherichia coli↗
PubMed1982

Serum resistance among Escherichia coli strains causing urinary tract infection in relation to O type and the carriage of hemolysin, colicin, and antibiotic resistance determinants.

The sensitivity to normal human serum of 91 smooth strains of Escherichia coli isolated from urinary tract infections was determined. Production of hemolysin, which was common and associated primarily with the types O4, O6, O18, and O75, was significantly correlated with high levels of serum resistance, both within the total population and within individual O types. In contrast, serum resistance was not significantly associated with antibiotic resistance (whether transmissible or not), with colicinogeny in general, or with colicin V production in particular. This indicates that the carriage of R and ColV plasmids, shown previously to be capable of conferring increased levels of serum resistance on individual strains of E. coli isolated from other sources, does not play an important part in determining the serum sensitivity of the E. coli population involved in urinary tract infection.

Anti-Bacterial Agents↗
PubMed1982

Hemolysin plasmid coding for the virulence of a nephropathogenic Escherichia coli strain.

The nephropathogenic Escherichia coli strain P673 was shown to harbor two plasmids with molecular sizes of 70 and 41 megadaltons, respectively. The 70-megadalton plasmid, pCW1, coded for tetracycline resistance, whereas hemolysin production was coded by the 41-megadalton plasmid, pCW2. Plasmid pCW1 proved to be self-transmissible, in contrast to pCW2. Transfer of the hemolysin character was associated with the appearance of a 110-megadalton plasmid, pCW3. The incompatibility of pCW3 with both native plasmids and restriction enzyme analysis led to the conclusion that pCW3 is a cointegrate of pCW1 and pCW2, pCW2, carrying the hemolytic determinant, is involved in the nephropathogenic character of strain P673, because (i) elimination of pCW2 from P673 was associated with a loss of virulence and (ii) the nephropathogenicity of the avirulent mutant could be restored by reintroduction of pCW2 DNA as part of a cointegrate structure.

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↗
PubMed1979

Plasmid cistrons controlling synthesis and excretion of the exotoxin alpha-haemolysin of Escherichia coli.

The synthesis and secretion of the toxic exoprotein alpha-haemolysin of E. coli PM152 is coded by the transmissible plasmid pHly152 (41 x 10(6) dalton) as shown by the transformation of the plasmid DNA and the isolation of mutants that are specifically altered in the synthesis and transport of haemolysin. These mutants were obtained by chemical mutagenesis and insertion of the ampicillin transposon (Tn3) into pHly152. Tn3 transposition was also used for the identification and the location of the cistrons on pHly152 essential for haemolysis. The EcoRI and HindIII fragments of the haemolytic plasmid pHly152 were cloned and used for the complementation of the haemolysis negative Tn3 insertion mutants. A DNA segment of 3.2 x 10(6) dalton could be thus identified which consists of at least three clustered cistrons necessary for haemolysis. Two of these cistrons are required for the formation of active haemolysin. At least one other cistron seems to be involved in the secretion of active haemolysin through the outer membrane of E. coli. The gene products determined by these cistrons were identified in minicells of E. coli. Their molecular properties were determined and their possible function in the formation and secretion of haemolysin will be discussed.

Escherichia coli↗
PubMed1987

The chromosomal fur gene regulates the extracellular haemolytic activity encoded by certain hly plasmids.

The haemolytic activity encoded by thirteen hly-plasmids of different origin and sources was examined as a function of the Fe3+-concentration in E. coli fur+ and E. coli fur- strains, respectively. In E. coli fur+ the relatively low haemolytic activity of five hly-plasmids isolated in Berne and one isolated in Paris was increased significantly under iron-limiting growth conditions. Contrastingly, in E. coli fur- strains containing the same plasmids, a considerably higher amount of secreted haemolysin was detected. This activity could not be further increased by limiting the extracellular iron concentration. Seven other hly-plasmids expressed similar and non-inducible amounts of secreted haemolysin in both E. coli fur+ and E. coli fur- strains. These results indicate that the extracellular haemolytic activity encoded by certain hly-plasmids was controlled by the chromosomally encoded fur gene.

Animals↗
PubMedDate not supplied

Salmonella typhimurium strains carrying haemolysin plasmids and cloned haemolysin genes from Escherichia coli.

Like all other Salmonella typhimurium strains examined, the smooth variants SF1397 (LT2) and 1366 and also their semi-rough and rough derivatives are non-haemolytic. Nevertheless, two haemolysin (Hly) plasmids of E. coli belonging to the inc groups incFIII,IV (pSU316) and incI2 (pHly152) were able to be introduced into these strains by conjugation and stably maintained. A considerable percentage of the Hly+ transconjugants obtained had lost parts of their O-side chains, a result of selection for the better recipient capability of "semi-rough" variants rather than the direct influence of the Hly+ plasmids themselves. In contrast to the incFIII,IV plasmid pSU316, which exhibited higher conjugation rates with rough recipients, the incI2 plasmid pHly152 was accepted best by smooth strains. Transformation with cloned E. coli haemolysin (hly) determinant was inefficient (less than 10(-6)) for smooth strains, but 10(2) - 10(3) times higher for rough recipients, and was increased by the use of Salmonella-modified DNA. The transformants and transconjugants were relatively stable and showed the same haemolytic activity as the E. coli donor strains. The virulence of the Hly+ smooth, semi-rough and rough S. typhimurium strains was tested in two mouse models, and neither the mortality rate nor the ability to multiply within the mouse spleen was influenced by the hly determinants.

Animals↗
PubMed1990

Secretion of the Bordetella pertussis adenylate cyclase from Escherichia coli containing the hemolysin operon.

The extracellular calmodulin-sensitive adenylate cyclase produced by Bordetella pertussis is synthesized as a 215-kDa precursor. This polypeptide is transported to the outer membrane of the bacteria where it is proteolytically processed to a 45-kDa catalytic subunit which is released into the culture supernatant [Masure, H.R., & Storm, D.R. (1989) biochemistry 28, 438-442]. The gene encoding this enzyme, cyaA, is part of the cya operon that also includes the genes cyaB, cyaD, and cyaE. A comparison of the predicted amino acid sequences encoded by cyaA, cyaB, and cyaD with the amino acid sequences encoded by hlyA, hlyB, and hlyD genes from the hemolysin (hly) operon from Escherichia coli shows a large degree of sequence similarity [Glaser, P., Sakamoto, H., Bellalou, J., Ullmann, A., & Danchin, A. (1988) EMBO J. 7, 3997-4004]. Complementation studies have shown that HlyB and HlyD are responsible for the secretion of HlyA (hemolysin) from E. coli. The signal sequence responsible for secretion of hemolysin has been shown to reside in its C-terminal 27 amino acids. Similarly, CyaB, CyaD, and CyaE are required for the secretion of CyaA from Bordetella pertussis. We placed the cyaA gene and a truncated cyaA gene that lacks the nucleotides that code for a putative C-terminal secretory signal sequence under the control of the lac promoter in the plasmid pUC-19. These plasmids were transformed into strains of E. coli which contained the hly operon. The truncated cyaA gene product, lacking the putative signal sequence, was not secreted but accumulated inside the cell.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenylyl Cyclases↗
PubMed1994

Binding to and killing of human renal epithelial cells by hemolytic P-fimbriated E. coli.

Acute pyelonephritis is a common invasive infection frequently caused by E. coli that possess P-fimbriae and secrete hemolysin. We have examined the role of P fimbriae and hemolysin in the killing of putative target cells of acute pyelonephritis, that is, human renal epithelial cells (HRPTEC). Cultures of HRPTEC were overlaid with (1) a prototypic pyelonephritogenic E. coli (CFT073) which expresses both P fimbriae and hemolysin; (2) its hemolysin-negative isogenic mutant (CFT073hlyD::TnphoA); or (3) a prototypic nonpyelonephritogenic fecal E. coli (FN414) which is negative for both P fimbriae and hemolysin. CFT073 and CFT073hlyD::TnphoA but not FN414 adhered to HRPTEC, as demonstrated by electron microscopy and direct counting. Adherence was diminished by antisera directed against P fimbriae and by a monoclonal antibody recognizing the epithelial receptor for P fimbriae. CFT073 was significantly more cytolethal for HRPTEC than its hemolysin-negative mutant. The bacteria-free filtrate of CFT073 was both hemolytic and cytolethal whereas that of CFT073hyD::TnphoA was not hemolytic and was significantly less cytolethal. Finally, we demonstrated that CFT073 passed through monolayers of HRPTEC at a higher rate than CFT073hlyD::TnphoA, indicating that hemolysin damages HRPTEC, facilitating passage of bacteria through the epithelial barrier. With HRPTEC and a pyelonephritogenic strain of E. coli we have reproduced in vitro bacterial attachment and toxin delivery by P fimbriae and hemolysin, factors epidemiologically associated with acute pyelonephritis in patients.

Bacterial Adhesion↗
PubMed1989

Cloning and characterization of a hemolysin gene from Actinobacillus (Haemophilus) pleuropneumoniae.

Neutralizing antisera to the leukotoxin secreted by Pasteurella haemolytica neutralized the hemolysin of Actinobacillus pleuropneumoniae and recognized a 110-kD antigen in cell-free culture supernatants from this organism. A series of nine overlapping recombinant phage clones carrying the gene for this 110-kD antigen were identified using affinity-purified anti-hemolysin antibody and a DNA probe containing sequences from the P. haemolytica lktCA genes. Eight of the nine clones expressed a 110-kD protein recognized by both anti-leukotoxin and anti-hemolysin antisera. The remaining clone expressed a truncated 80-kD antigen which was also recognized by both antisera. Sequence analysis of a region of the cloned DNA revealed two open reading frames encoding proteins with predicted masses of 18.5 and 102.5 kD. These genes, which we designate appC and appA, respectively, are similar in sequence to the hlyCA genes of Escherichia coli and the lktCA genes of P. haemolytica. Hemolytic activity could be detected in lysates of E. coli harboring plasmids containing the appCa genes.

Actinobacillus↗
PubMed1989

Specificity of insertion of IS91, an insertion sequence present in alpha-haemolysin plasmids of Escherichia coli.

We have determined the DNA sequences of eight different insertions of IS91 in a specifically engineered recipient plasmid of known DNA sequence (pSU300). The sequences at the termini of IS91 are 5'-CGAGTAGG...CCTATCGAT. IS91 inserts specifically 5' to either one of the tetranucleotides 5'-GAAC or 5'-CAAG, and always in the same relative orientation with respect to the sequence of the target. Except in one special case, no duplications of the recipient DNA were produced at the site of insertion.

Bacterial Proteins↗
PubMed1983

Cloned hemolysin genes from Escherichia coli that cause urinary tract infection determine different levels of toxicity in mice.

After intraperitoneal injection of mice with Escherichia coli strains isolated from patients with urinary tract infections, the mortality due to hemolytic (Hly+) and nonhemolytic (Hly-) isolates was 77 and 40%, respectively. Deletion of the chromosomal hemolysin (hly) determinant in an E. coli O6:K15:H31 urinary tract infection strain led to a significant reduction in toxicity for mice, and its reintroduction on a recombinant plasmid partially restored the original toxicity. Although introduction of the cloned plasmid pHly152-encoded hly determinant into the Hly- E. coli O6 mutant strain increased toxicity by only a marginal degree, transformation with the cloned chromosomal hly determinants from two E. coli strains of serotypes O18ac:K5:H- and O75:K95:H? resulted in markedly greater toxicity, even exceeding that of the original Hly+ E. coli O6 wild-type strain.

Animals↗