Antiproliferative and Antimicrobial Potentials of a Lectin from <i>Aplysia kurodai</i> (Sea Hare) Eggs

In recent years, there has been considerable interest in lectins from marine invertebrates. In this study, the biological activities of a lectin protein isolated from the eggs of Sea hare (<i>Aplysia kurodai</i>) were evaluated. The 40 kDa <i>Aplysia kurodai</i> egg lectin (o...

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Main Authors: Rubaiya Rafique Swarna, A. K. M. Asaduzzaman, Syed Rashel Kabir, Nawshin Arfin, Sarkar M. A. Kawsar, Sultana Rajia, Yuki Fujii, Yukiko Ogawa, Keisuke Hirashima, Nanae Kobayashi, Masao Yamada, Yasuhiro Ozeki, Imtiaj Hasan
Format: Article
Language:English
Published: MDPI AG 2021-07-01
Series:Marine Drugs
Subjects:
Online Access:https://www.mdpi.com/1660-3397/19/7/394
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author Rubaiya Rafique Swarna
A. K. M. Asaduzzaman
Syed Rashel Kabir
Nawshin Arfin
Sarkar M. A. Kawsar
Sultana Rajia
Yuki Fujii
Yukiko Ogawa
Keisuke Hirashima
Nanae Kobayashi
Masao Yamada
Yasuhiro Ozeki
Imtiaj Hasan
author_facet Rubaiya Rafique Swarna
A. K. M. Asaduzzaman
Syed Rashel Kabir
Nawshin Arfin
Sarkar M. A. Kawsar
Sultana Rajia
Yuki Fujii
Yukiko Ogawa
Keisuke Hirashima
Nanae Kobayashi
Masao Yamada
Yasuhiro Ozeki
Imtiaj Hasan
author_sort Rubaiya Rafique Swarna
collection DOAJ
description In recent years, there has been considerable interest in lectins from marine invertebrates. In this study, the biological activities of a lectin protein isolated from the eggs of Sea hare (<i>Aplysia kurodai</i>) were evaluated. The 40 kDa <i>Aplysia kurodai</i> egg lectin (or AKL-40) binds to D-galacturonic acid and D-galactose sugars similar to previously purified isotypes with various molecular weights (32/30 and 16 kDa). The N-terminal sequence of AKL-40 was similar to other sea hare egg lectins. The lectin was shown to be moderately toxic to brine shrimp nauplii, with an LC<sub>50</sub> value of 63.63 µg/mL. It agglutinated Ehrlich ascites carcinoma cells and reduced their growth, up to 58.3% in vivo when injected into Swiss albino mice at a rate of 2 mg/kg/day. The morphology of these cells apparently changed due to AKL-40, while the expression of apoptosis-related genes (p53, Bax, and Bcl-XL) suggested a possible apoptotic pathway of cell death. AKL-40 also inhibited the growth of human erythroleukemia cells, probably via activating the MAPK/ERK pathway, but did not affect human B-lymphoma cells (Raji) or rat basophilic leukemia cells (RBL-1). In vitro, lectin suppressed the growth of Ehrlich ascites carcinoma and U937 cells by 37.9% and 31.8%, respectively. Along with strong antifungal activity against <i>Talaromyces verruculosus</i>, AKL showed antibacterial activity against <i>Staphylococcus aureus</i>, <i>Shigella sonnei</i>, and <i>Bacillus cereus</i> whereas the growth of <i>Escherichia coli</i> was not affected by the lectin. This study explores the antiproliferative and antimicrobial potentials of AKL as well as its involvement in embryo defense of sea hare.
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spelling doaj.art-eb27c5a5d9574c6abf01fce8a5c2116b2023-11-22T04:14:17ZengMDPI AGMarine Drugs1660-33972021-07-0119739410.3390/md19070394Antiproliferative and Antimicrobial Potentials of a Lectin from <i>Aplysia kurodai</i> (Sea Hare) EggsRubaiya Rafique Swarna0A. K. M. Asaduzzaman1Syed Rashel Kabir2Nawshin Arfin3Sarkar M. A. Kawsar4Sultana Rajia5Yuki Fujii6Yukiko Ogawa7Keisuke Hirashima8Nanae Kobayashi9Masao Yamada10Yasuhiro Ozeki11Imtiaj Hasan12Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, BangladeshDepartment of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, BangladeshDepartment of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, BangladeshDepartment of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, BangladeshDepartment of Chemistry, University of Chittagong, Chittagong 4331, BangladeshCenter for Interdisciplinary Research, Varendra University, Rajshahi 6204, BangladeshGraduate School of Pharmaceutical Sciences, Nagasaki International University, 2825-7, Huis Ten Bosch-cho, Sasebo, Nagasaki 859-3298, JapanGraduate School of Pharmaceutical Sciences, Nagasaki International University, 2825-7, Huis Ten Bosch-cho, Sasebo, Nagasaki 859-3298, JapanSchool of Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, JapanSchool of Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, JapanSchool of Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, JapanSchool of Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, JapanDepartment of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, BangladeshIn recent years, there has been considerable interest in lectins from marine invertebrates. In this study, the biological activities of a lectin protein isolated from the eggs of Sea hare (<i>Aplysia kurodai</i>) were evaluated. The 40 kDa <i>Aplysia kurodai</i> egg lectin (or AKL-40) binds to D-galacturonic acid and D-galactose sugars similar to previously purified isotypes with various molecular weights (32/30 and 16 kDa). The N-terminal sequence of AKL-40 was similar to other sea hare egg lectins. The lectin was shown to be moderately toxic to brine shrimp nauplii, with an LC<sub>50</sub> value of 63.63 µg/mL. It agglutinated Ehrlich ascites carcinoma cells and reduced their growth, up to 58.3% in vivo when injected into Swiss albino mice at a rate of 2 mg/kg/day. The morphology of these cells apparently changed due to AKL-40, while the expression of apoptosis-related genes (p53, Bax, and Bcl-XL) suggested a possible apoptotic pathway of cell death. AKL-40 also inhibited the growth of human erythroleukemia cells, probably via activating the MAPK/ERK pathway, but did not affect human B-lymphoma cells (Raji) or rat basophilic leukemia cells (RBL-1). In vitro, lectin suppressed the growth of Ehrlich ascites carcinoma and U937 cells by 37.9% and 31.8%, respectively. Along with strong antifungal activity against <i>Talaromyces verruculosus</i>, AKL showed antibacterial activity against <i>Staphylococcus aureus</i>, <i>Shigella sonnei</i>, and <i>Bacillus cereus</i> whereas the growth of <i>Escherichia coli</i> was not affected by the lectin. This study explores the antiproliferative and antimicrobial potentials of AKL as well as its involvement in embryo defense of sea hare.https://www.mdpi.com/1660-3397/19/7/394antibacterial activityanticancer activityantifungal activity<i>Aplysia kurodai</i>apoptosisEhrlich ascites carcinoma
spellingShingle Rubaiya Rafique Swarna
A. K. M. Asaduzzaman
Syed Rashel Kabir
Nawshin Arfin
Sarkar M. A. Kawsar
Sultana Rajia
Yuki Fujii
Yukiko Ogawa
Keisuke Hirashima
Nanae Kobayashi
Masao Yamada
Yasuhiro Ozeki
Imtiaj Hasan
Antiproliferative and Antimicrobial Potentials of a Lectin from <i>Aplysia kurodai</i> (Sea Hare) Eggs
Marine Drugs
antibacterial activity
anticancer activity
antifungal activity
<i>Aplysia kurodai</i>
apoptosis
Ehrlich ascites carcinoma
title Antiproliferative and Antimicrobial Potentials of a Lectin from <i>Aplysia kurodai</i> (Sea Hare) Eggs
title_full Antiproliferative and Antimicrobial Potentials of a Lectin from <i>Aplysia kurodai</i> (Sea Hare) Eggs
title_fullStr Antiproliferative and Antimicrobial Potentials of a Lectin from <i>Aplysia kurodai</i> (Sea Hare) Eggs
title_full_unstemmed Antiproliferative and Antimicrobial Potentials of a Lectin from <i>Aplysia kurodai</i> (Sea Hare) Eggs
title_short Antiproliferative and Antimicrobial Potentials of a Lectin from <i>Aplysia kurodai</i> (Sea Hare) Eggs
title_sort antiproliferative and antimicrobial potentials of a lectin from i aplysia kurodai i sea hare eggs
topic antibacterial activity
anticancer activity
antifungal activity
<i>Aplysia kurodai</i>
apoptosis
Ehrlich ascites carcinoma
url https://www.mdpi.com/1660-3397/19/7/394
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