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.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
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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.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1999
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