A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis
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...
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MDPI AG
2014-09-01
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| Series: | Molecules |
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| Online Access: | http://www.mdpi.com/1420-3049/19/9/13990 |
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| author | Imtiaj Hasan Miharu Watanabe Naoto Ishizaki Yoshiko Sugita-Konishi Yasushi Kawakami Jun Suzuki Chikaku Dogasaki Sultana Rajia Sarkar M. A. Kawsar Yasuhiro Koide Robert A. Kanaly Shigeki Sugawara Masahiro Hosono Yukiko Ogawa Yuki Fujii Hideyuki Iriko Jiharu Hamako Taei Matsui Yasuhiro Ozeki |
| author_facet | Imtiaj Hasan Miharu Watanabe Naoto Ishizaki Yoshiko Sugita-Konishi Yasushi Kawakami Jun Suzuki Chikaku Dogasaki Sultana Rajia Sarkar M. A. Kawsar Yasuhiro Koide Robert A. Kanaly Shigeki Sugawara Masahiro Hosono Yukiko Ogawa Yuki Fujii Hideyuki Iriko Jiharu Hamako Taei Matsui Yasuhiro Ozeki |
| author_sort | Imtiaj Hasan |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-11T11:00:47Z |
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| id | doaj.art-9c02d8e22fe34b2e891c95b60927b3d4 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-11T11:00:47Z |
| publishDate | 2014-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-9c02d8e22fe34b2e891c95b60927b3d42022-12-22T01:09:53ZengMDPI AGMolecules1420-30492014-09-01199139901400310.3390/molecules190913990molecules190913990A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced HemolysisImtiaj Hasan0Miharu Watanabe1Naoto Ishizaki2Yoshiko Sugita-Konishi3Yasushi Kawakami4Jun Suzuki5Chikaku Dogasaki6Sultana Rajia7Sarkar M. A. Kawsar8Yasuhiro Koide9Robert A. Kanaly10Shigeki Sugawara11Masahiro Hosono12Yukiko Ogawa13Yuki Fujii14Hideyuki Iriko15Jiharu Hamako16Taei Matsui17Yasuhiro Ozeki18Laboratories 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, JapanSchool of Life and Environmental Science, Azabu University, 1-17-71, Fuchinobe, Chuo-ku, Sagamihara, Kanagawa 252-5201, JapanSchool of Life and Environmental Science, Azabu University, 1-17-71, Fuchinobe, Chuo-ku, Sagamihara, Kanagawa 252-5201, JapanSchool of Life and Environmental Science, Azabu University, 1-17-71, Fuchinobe, Chuo-ku, Sagamihara, Kanagawa 252-5201, JapanSchool of Life and Environmental Science, Azabu University, 1-17-71, Fuchinobe, Chuo-ku, Sagamihara, Kanagawa 252-5201, JapanSchool of Life and Environmental Science, Azabu University, 1-17-71, Fuchinobe, Chuo-ku, Sagamihara, Kanagawa 252-5201, JapanSchool of Life and Environmental Science, Azabu University, 1-17-71, Fuchinobe, Chuo-ku, Sagamihara, Kanagawa 252-5201, JapanLaboratories 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, JapanDepartment of Chemistry, Faculty of Sciences, University of Chittagong, Chittagong-4331, BangladeshLaboratories 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, JapanLaboratories 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, JapanDivision of Cell Recognition Study, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai 981-8558, JapanDivision of Cell Recognition Study, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai 981-8558, JapanDepartment of Pharmacy, Faculty of Pharmaceutical Science, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo, Nagasaki 859-3298, JapanDepartment of Pharmacy, Faculty of Pharmaceutical Science, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo, Nagasaki 859-3298, JapanDepartment of Parasitology, Graduate School of Health Sciences, Kobe University, 7-10-2, Tomogaoka, Suma-ku, Kobe 654-0142, JapanDepartment of Biology, School of Health Sciences, Fujita Health University, Toyoake, Aichi 470-1192, JapanDepartment of Biology, School of Health Sciences, Fujita Health University, Toyoake, Aichi 470-1192, JapanLaboratories 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, JapanA 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.http://www.mdpi.com/1420-3049/19/9/13990Aplysia kurodailectinhemolysissea hare eggslectinStreptococcus pyogenesstreptolysin |
| spellingShingle | Imtiaj Hasan Miharu Watanabe Naoto Ishizaki Yoshiko Sugita-Konishi Yasushi Kawakami Jun Suzuki Chikaku Dogasaki Sultana Rajia Sarkar M. A. Kawsar Yasuhiro Koide Robert A. Kanaly Shigeki Sugawara Masahiro Hosono Yukiko Ogawa Yuki Fujii Hideyuki Iriko Jiharu Hamako Taei Matsui Yasuhiro Ozeki A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis Molecules Aplysia kurodai lectin hemolysis sea hare eggs lectin Streptococcus pyogenes streptolysin |
| title | A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis |
| title_full | A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis |
| title_fullStr | A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis |
| title_full_unstemmed | A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis |
| title_short | A Galactose-Binding Lectin Isolated from Aplysia kurodai (Sea Hare) Eggs Inhibits Streptolysin-Induced Hemolysis |
| title_sort | galactose binding lectin isolated from aplysia kurodai sea hare eggs inhibits streptolysin induced hemolysis |
| topic | Aplysia kurodai lectin hemolysis sea hare eggs lectin Streptococcus pyogenes streptolysin |
| url | http://www.mdpi.com/1420-3049/19/9/13990 |
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