TITLE

Characterization of the Interaction of Hemolytic Lectin CEL-III from the Marine Invertebrate, Cucumaria echinata, with Artificial Lipid Membranes: Involvement of Neutral Sphingoglycolipids in the Pore-Forming Process1

AUTHOR(S)
Hatakeyama, Tomomitsu; Sato, Taiji; Taira, Etsuyo; Kuwahara, Hiromiki; Niidome, Takuro; Aoyagi, Haruhiko
PUB. DATE
January 1999
SOURCE
Journal of Biochemistry;1999, Vol. 125 Issue 2, p277
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The hemolytic lectin, CEL-III, is a Ca2+-dependent, galactose/N-acetylgalactosamine-specific lectin purified from the marine invertebrate, Cucumaria echinata (Holothuroidea). After binding to specific carbohydrates on the erythrocyte surface, CEL-III forms ion-permeable pores by oligomerizing in the membrane, which leads to colloid osmotic rupture of the cells. When incubated with liposomes composed of total lipids from the human erythrocyte membrane, CEL-III efficiently induced the leakage of carboxyfluorescein (CF) trapped in the vesicles, suggesting the presence of its receptor in the membrane lipids. The rate of CF-leakage increased with increasing temperature, although the hemolytic activity of CEL-III had been found to be much higher at lower temperatures (around 10C). Identification of the receptor for CEL-III was performed by examining the ability of individual lipids from human erythrocytes to induce CF-leakage from DOPC-liposomes. As a result, the most effective receptor was found to be lactosyl ceramide (LacCer), while globoside (Gb4Cer) also showed slight induction of CF-leakage. On the other hand, a binding assay involving CEL-III-horseradish peroxidase conjugate indicated that CEL-III exhibits similar affinity for LacCer and Gb4Cer, suggesting that the structure or length of the carbohydrate portion of sphingoglycolipids is also relevant as to their ability to induce CF-leakage in addition to their affinity. Electron micrographs of CEL-III-treated liposomes revealed that CEL-III induced considerable morphological changes in the vesicles, while a clearly distinguishable oligomeric structure of the protein was not observed.
ACCESSION #
82066692

 

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