A mechanism of resistance to hydrogen peroxide in Vibrio rumoiensis S-1.
A possible mechanism of resistance to hydrogen peroxide (H2O2) in Vibrio rumoiensis, isolated from the H2O2-rich drain pool of a fish processing plant, was examined. When V. rumoiensis cells were inoculated into medium containing either 5 mM or no H2O2, they grew in similar manners. A spontaneous mutant strain, S-4, derived from V. rumoiensis and lacking catalase activity did not grow at all in the presence of 5 mM H2O2. These results suggest that catalase is inevitably involved in the resistance and survival of V. rumoiensis in the presence of H2O2. Catalase activity was constitutively present in V. rumoiensis cells grown in the absence of H2O2, and its occurrence was dependent on the age of the cells, a characteristic which is observed for the HP II-type catalase of Escherichia coli. The presence of the HP II-type catalase in V. rumoiensis cells was evidenced by partial sequencing of the gene encoding the HP II-type catalase from this organism. A notable difference between V. rumoiensis and E. coli is that catalase is accumulated at very high levels ( approximately 2% of the total soluble proteins) in V. rumoiensis, in contrast to the case for E. coli. When V. rumoiensis cells which had been exposed to 5 mM H2O2 were centrifuged, most intracellular proteins, including catalase, were recovered in the medium. On the other hand, when V. rumoiensis cells were grown on plates containing various concentrations of H2O2, individual cells had a colony-forming ability inferior to those of E. coli, Bacillus subtilis, and Vibrio parahaemolyticus. Thus, it is suggested that when V. rumoiensis cells are exposed to high concentrations of H2O2, most cells will immediately be broken by H2O2. In addition, the cells which have had little or no damage will start to grow in a medium where almost all H2O2 has been decomposed by the catalase released from broken cells.
Ichise
N
N
Laboratory of Environmental Molecular Biology, Graduate School of Environmental Earth Science, Hokkaido University, Kita-ku, Sapporo 060-0810, Japan.
Morita
N
N
Hoshino
T
T
Kawasaki
K
K
Yumoto
I
I
Okuyama
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002374:Catalase / Q000235:genetics / Q000378:metabolism; D017931:DNA Primers / Q000235:genetics; D004352:Drug Resistance, Microbial / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005399:Fishes; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D014733:Vibrio / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D014871:Water Microbiology
D017931:DNA Primers; D006861:Hydrogen Peroxide; D002374:Catalase