Papers

Peer-reviewed
1997

Analysis of the Structural Gene Encoding a Hemolysin in Vibrio mimicus

Japanese Journal of Microbiology
  • Rahman Md. Monzur
  • ,
  • Miyoshi Shin-ichi
  • ,
  • Tomochika Ken-ichi
  • ,
  • Wakae Hitoshi
  • ,
  • Shinoda Sumio

Volume
41
Number
2
First page
169
Last page
173
Language
English
Publishing type
Publisher
Center For Academic Publications Japan

An environmental isolate of V. mimicus, strain E-33, has been reported to produce and secrete a hemolysin of 63kDa. The hemolysin is enterotoxic in test animals. The nucleotide sequence of the structural gene of the hemolysin was determined. We found a 2, 232bp open reading frame, which codes a peptide of 744 amino acids, with a calculated molecular weight of 83, 903 Da. The sequence for the structural gene was closely related to the V. cholerae el for hlyA gene, coding an exocellular hemolysin. The amino terminal amino-acid sequence of the 63kDa hemolysin, purified from V. mimicus, was determined by the Edman degradation method and found to be NH2=-S-V-S-A-N-N-V-T-N-N-N-E-T. This sequence is identical from S-152 to T-164 predicted from the nucleotide sequence. So, it seems that the mature hemolysin in V. mimicus is processed upon deleting the first 151 amino acids, and the molecular mass is 65, 972 Da. Analyzing the deduced amino-acid sequence, we also found a potential signal sequence of 24 amino acids at the amino terminal. Our results suggest that, like V. cholerae hemolysin, two-step processing also exists in V. mimicus hemolysin.

Link information
CiNii Articles
http://ci.nii.ac.jp/naid/130003484484
URL
https://jlc.jst.go.jp/DN/JALC/00083456893?from=CiNii
ID information
  • ISSN : 0385-5600
  • CiNii Articles ID : 130003484484

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