BIOMAT Database Logo BIOMAT Database Logo

Purification and characterization of enterotoxin produced by Aeromonas sobria. 1998

Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Institute of Pharmacognosy, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima, Japan.

We purified the toxin of Aeromonas sobria capable of inducing a positive response in the mouse intestinal loop assay. The purified toxin showed a positive response not only in the loop assay but also in a hemolytic assay. Subsequently, we cloned the toxin gene and demonstrated that the product of this gene possessed both hemolytic and enterotoxic activities. These results showed that the enterotoxin of A. sobria possesses hemolytic activity. Nucleotide sequence determination of the toxin gene and amino acid sequence analysis of the purified toxin revealed that it is synthesized as a precursor composed of 488 amino acid residues, and that the 24 amino-terminal amino acid residues of the precursor is removed in the mature toxin. As antiserum against the purified toxin neutralized the fluid accumulation induced by living cells not only of A. sobria but also of A. hydrophila, this and antigenically related toxin(s) are thought to play an essential role in the induction of diarrhea by these organisms. The toxin-injured Chinese hamster ovary (CHO) cells induced the release of intracellular lactose dehydrogenase (LDH). The release of LDH from CHO cells and the lysis of erythrocytes by the toxin were repressed by the addition of dextran to the reaction solution, indicating that the toxin forms pores in the membranes and that the cells were injured by the osmotic gradient developed due to pore formation. However, the histopathological examination of intestinal cells exposed to the toxin showed that it caused fluid accumulation in the mouse intestinal loop without causing cellular damage.

UI MeSH Term Description Entries
D007422 Intestines The section of the alimentary canal from the STOMACH to the ANAL CANAL. It includes the LARGE INTESTINE and SMALL INTESTINE. Intestine
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D003967 Diarrhea An increased liquidity or decreased consistency of FECES, such as running stool. Fecal consistency is related to the ratio of water-holding capacity of insoluble solids to total water, rather than the amount of water present. Diarrhea is not hyperdefecation or increased fecal weight. Diarrheas
D004768 Enterotoxins Substances that are toxic to the intestinal tract causing vomiting, diarrhea, etc.; most common enterotoxins are produced by bacteria. Staphylococcal Enterotoxin,Enterotoxin,Staphylococcal Enterotoxins,Enterotoxin, Staphylococcal,Enterotoxins, Staphylococcal
D005798 Genes, Bacterial The functional hereditary units of BACTERIA. Bacterial Gene,Bacterial Genes,Gene, Bacterial
D006224 Cricetinae A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. Cricetus,Hamsters,Hamster
D006460 Hemolysin Proteins Proteins from BACTERIA and FUNGI that are soluble enough to be secreted to target ERYTHROCYTES and insert into the membrane to form beta-barrel pores. Biosynthesis may be regulated by HEMOLYSIN FACTORS. Hemolysin,Hemolysins,Hemalysins,Proteins, Hemolysin
D000333 Aeromonas A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that occurs singly, in pairs, or in short chains. Its organisms are found in fresh water and sewage and are pathogenic to humans, frogs, and fish.
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

Related Publications

Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Purification and characterization of cytolytic toxins produced by Aeromonas hydrophila and Aeromonas veronii biotype sobria strains.
January 2006, Polish journal of microbiology,
Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Purification of cytotoxic enterotoxin of Aeromonas sobria by use of monoclonal antibodies.
March 1987, Journal of medical microbiology,
Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Purification and partial characterization of a cytotonic enterotoxin produced by Aeromonas hydrophila.
July 1989, Canadian journal of microbiology,
Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Isolation and purification of Aeromonas sobria cytotonic enterotoxin and beta-haemolysin.
March 1993, Journal of medical microbiology,
Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Purification and characterization of lipase from Aeromonas sobria LP004.
April 1997, Journal of biotechnology,
Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Maturation pathway of metalloprotease produced by Aeromonas sobria.
October 2010, Microbiology and immunology,
Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Purification and characterization of Aeromonas sobria pili, a possible colonization factor.
October 1991, Infection and immunity,
Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Hyperproduction, purification, and mechanism of action of the cytotoxic enterotoxin produced by Aeromonas hydrophila.
October 1997, Infection and immunity,
Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
[Purification and characterization of hec toxin produced by Aeromonas hydrophila].
December 1992, Wei sheng wu xue bao = Acta microbiologica Sinica,
Y Fujii, and T Nomura, and H Kanzawa, and M Kameyama, and H Yamanaka, and M Akita, and K Setsu, and K Okamoto
Purification and characterization of Aeromonas sobria Ae24 pili: a possible new colonization factor.
October 1992, Microbial pathogenesis,
Copied contents to your clipboard!