Elsevier

Toxicon

Volume 33, Issue 5, May 1995, Pages 651-657
Toxicon

The binding of Vibrio parahaemolyticus 125I-labeled thermostable direct hemolysin to erythrocytes

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Abstract

Thermostable direct hemolysin (TDH) produced by Vibrio parahaemolyticus was iodinated using chloramine T. The 125I-labeled TDH retained up to 80% of the activity of intact toxin. The binding of 125I-TDH to rabbit erythrocytes was inhibited by addition of nonlabeled TDH. The binding of 125I-TDH to rabbit erythrocytes was completed in the 1st or 2nd min of incubation at 37 °C in contrast to that at 4 °C. 125I-TDH, which cannot lyse horse erythrocytes as does intact TDH, bound to horse erythrocytes as to those of rabbit. The dissociation constants (KD) derived from Scatchard plots were 2.85, 4.39, 4.33 and 5.35 × 10−8 M for rabbit, horse, human and sheep erythrocytes, respectively. The lytic sensitivity of various erythrocytes to TDH showed no relationship to the binding capacity.

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Cited by (10)

  • Structure, function and regulation of the thermostable direct hemolysin (TDH) in pandemic Vibrio parahaemolyticus

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    The imbalance of ions inside and outside of the cells causes membrane permeabilization and erythrocytes to swell, leading to lysis [34,35]. GT1 ganglioside was thought to be the receptor sites for TDH on erythrocyte membranes [36,37], however other studies reported contradictory results [38–40]. TDH has been observed to exhibit cytotoxicity in a variety of cell lines [41–44].

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