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Correction published on 21 January 2016, see Molecules 2016, 21(1), 129.
Open AccessArticle

A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis

1
Laboratories of Glycobiology & Marine Biochemistry and Molecular Toxicology, Department of Life and Environmental System Science, Graduate School of NanoBio Sciences, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan
2
School of Life and Environmental Science, Azabu University, 1-17-71, Fuchinobe, Chuo-ku, Sagamihara, Kanagawa 252-5201, Japan
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Department of Biochemistry and Molecular Biology, Faculty of Science, University of Rajshahi, Rajshahi-6205, Bangladesh
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Department of Natural Science, Varendra University, Rajshahi-6204, Bangladesh
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Department of Chemistry, Faculty of Sciences, University of Chittagong, Chittagong-4331, Bangladesh
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Division of Cell Recognition Study, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai 981-8558, Japan
7
Department of Pharmacy, Faculty of Pharmaceutical Science, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo, Nagasaki 859-3298, Japan
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Department of Parasitology, Graduate School of Health Sciences, Kobe University, 7-10-2, Tomogaoka, Suma-ku, Kobe 654-0142, Japan
9
Department of Biology, School of Health Sciences, Fujita Health University, Toyoake, Aichi 470-1192, Japan
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Molecules 2014, 19(9), 13990-14003; https://doi.org/10.3390/molecules190913990
Received: 13 July 2014 / Revised: 21 August 2014 / Accepted: 2 September 2014 / Published: 5 September 2014
(This article belongs to the Special Issue Lectins)
A specific galactose-binding lectin was shown to inhibit the hemolytic effect of streptolysin O (SLO), an exotoxin produced by Streptococcus pyogenes. Commercially available lectins that recognize N-acetyllactosamine (ECA), T-antigen (PNA), and Tn-antigen (ABA) agglutinated rabbit erythrocytes, but had no effect on SLO-induced hemolysis. In contrast, SLO-induced hemolysis was inhibited by AKL, a lectin purified from sea hare (Aplysia kurodai) eggs that recognizes α-galactoside oligosaccharides. This inhibitory effect was blocked by the co-presence of d-galactose, which binds to AKL. A possible explanation for these findings is that cholesterol-enriched microdomains containing glycosphingolipids in the erythrocyte membrane become occupied by tightly stacked lectin molecules, blocking the interaction between cholesterol and SLO that would otherwise result in penetration of the membrane. Growth of S. pyogenes was inhibited by lectins from a marine invertebrate (AKL) and a mushroom (ABA), but was promoted by a plant lectin (ECA). Both these inhibitory and promoting effects were blocked by co-presence of galactose in the culture medium. Our findings demonstrate the importance of glycans and lectins in regulating mechanisms of toxicity, creation of pores in the target cell membrane, and bacterial growth. View Full-Text
Keywords: Aplysia kurodai; lectin; hemolysis; sea hare eggs; lectin; Streptococcus pyogenes; streptolysin Aplysia kurodai; lectin; hemolysis; sea hare eggs; lectin; Streptococcus pyogenes; streptolysin
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Hasan, I.; Watanabe, M.; Ishizaki, N.; Sugita-Konishi, Y.; Kawakami, Y.; Suzuki, J.; Dogasaki, C.; Rajia, S.; Kawsar, S.M.A.; Koide, Y.; Kanaly, R.A.; Sugawara, S.; Hosono, M.; Ogawa, Y.; Fujii, Y.; Iriko, H.; Hamako, J.; Matsui, T.; Ozeki, Y. A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis. Molecules 2014, 19, 13990-14003.

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