Inactivation of two haemolytic toxin genes in Aeromonas hydrophila attenuates virulence in a suckling mouse model

Article Abstract:

The virulence of two unrelated Aeromonas hydrophila beta-hemolytic toxins was investigated in a suckling mouse model. The first hemolysin gene, extracted from an A. hydrophila A6 cosmid bank, encoded a possible gene product of 621 amino acids with a molecular size of 69.0 kDa. The inferred amino acid sequence had an 89% similarity to the AHH1 hemolysin of A. hydrophila ATCC 7966 and 51% identity with the HlyA hemolysin of Vibrio cholerae El Tor strain O17. The second hemolysin gene encodes aerolysin, a pore-forming toxin, was partially cloned. It is suggested that the 69.0 kDa V. cholerae-Hly-A-like hemolysin gene be called hlyA in contrast with the second one called aerA.

Gram-negative bacteria, Bacterial toxins, Hemolysis and hemolysins, Virulence (Microbiology), Hemolysis

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A novel copper-binding protein with characteristics of a metallothionein from a clinical isolate of Candida albicans

Article Abstract:

A novel copper-binding protein from a clinical isolate of Candida albicans is discussed. The protein has characteristics of a metallothionein (MT). The copper/protein ratio went up steadily through the purification steps. The amino-terminal segment of the protein had three Cys-Xaa-Cys motifs as a metallothionein would and significant homology with mammalian MTs was seen relative to the positions of the cysteine residues.

Japan, Statistical Data Included, Physiological aspects, Carrier proteins, Transport proteins, Cytochemistry, Copper, Metallothionein, Candida albicans

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