{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,4]],"date-time":"2026-07-04T14:42:11Z","timestamp":1783176131150,"version":"3.54.6"},"reference-count":56,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2021,7,14]],"date-time":"2021-07-14T00:00:00Z","timestamp":1626220800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP19K06239"],"award-info":[{"award-number":["JP19K06239"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>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 (Aplysia kurodai) were evaluated. The 40 kDa Aplysia kurodai 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 LC50 value of 63.63 \u00b5g\/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 Talaromyces verruculosus, AKL showed antibacterial activity against Staphylococcus aureus, Shigella sonnei, and Bacillus cereus whereas the growth of Escherichia coli 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.<\/jats:p>","DOI":"10.3390\/md19070394","type":"journal-article","created":{"date-parts":[[2021,7,14]],"date-time":"2021-07-14T10:13:42Z","timestamp":1626257622000},"page":"394","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Antiproliferative and Antimicrobial Potentials of a Lectin from Aplysia kurodai (Sea Hare) Eggs"],"prefix":"10.3390","volume":"19","author":[{"given":"Rubaiya Rafique","family":"Swarna","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, Bangladesh"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9182-3456","authenticated-orcid":false,"given":"A. K. M.","family":"Asaduzzaman","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, Bangladesh"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5708-014X","authenticated-orcid":false,"given":"Syed Rashel","family":"Kabir","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, Bangladesh"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nawshin","family":"Arfin","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, Bangladesh"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7964-9117","authenticated-orcid":false,"given":"Sarkar M. A.","family":"Kawsar","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Chittagong, Chittagong 4331, Bangladesh"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sultana","family":"Rajia","sequence":"additional","affiliation":[{"name":"Center for Interdisciplinary Research, Varendra University, Rajshahi 6204, Bangladesh"},{"name":"School of Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6408-9620","authenticated-orcid":false,"given":"Yuki","family":"Fujii","sequence":"additional","affiliation":[{"name":"Graduate School of Pharmaceutical Sciences, Nagasaki International University, 2825-7, Huis Ten Bosch-cho, Sasebo, Nagasaki 859-3298, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yukiko","family":"Ogawa","sequence":"additional","affiliation":[{"name":"Graduate School of Pharmaceutical Sciences, Nagasaki International University, 2825-7, Huis Ten Bosch-cho, Sasebo, Nagasaki 859-3298, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keisuke","family":"Hirashima","sequence":"additional","affiliation":[{"name":"School of Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nanae","family":"Kobayashi","sequence":"additional","affiliation":[{"name":"School of Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan"},{"name":"School of Medicine, Yokohama City University, 3-9, Fukuura, Kanazawa-ku, Yokohama 236-0004, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masao","family":"Yamada","sequence":"additional","affiliation":[{"name":"School of Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2782-6158","authenticated-orcid":false,"given":"Yasuhiro","family":"Ozeki","sequence":"additional","affiliation":[{"name":"School of Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4715-9022","authenticated-orcid":false,"given":"Imtiaj","family":"Hasan","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, Bangladesh"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,7,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"44772","DOI":"10.1074\/jbc.M112.418012","article-title":"A lectin from the mussel Mytilus galloprovincialis has a highly novel primary structure and induces glycan-mediated cytotoxicity of globotriaosylceramide-expressing lymphoma cells","volume":"287","author":"Fujii","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"14450","DOI":"10.1074\/jbc.273.23.14450","article-title":"Novel galactose-binding proteins in Annelida. Characterization of 29-kDa tandem repeat-type lectins from the earthworm Lumbricus terrestris","volume":"273","author":"Hirabayashi","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.cbpc.2005.10.019","article-title":"A beta-galactose-specific lectin isolated from the marine worm Chaetopterus variopedatus possesses anti-HIV-1 activity","volume":"142","author":"Wang","year":"2006","journal-title":"Comp. Biochem. Physiol. C Toxicol. Pharmacol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.fsi.2008.01.002","article-title":"Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)","volume":"24","author":"Gowda","year":"2008","journal-title":"Fish Shellfish Immunol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/j.ijbiomac.2018.11.222","article-title":"Histochemical localization of N-acetylhexosamine-binding lectin HOL-18 in Halichondria okadai (Japanese black sponge), and its antimicrobial and cytotoxic anticancer effects","volume":"124","author":"Hasan","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/j.cell.2006.08.019","article-title":"Glycosylation in cellular mechanisms of health and disease","volume":"126","author":"Ohtsubo","year":"2006","journal-title":"Cell"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"364","DOI":"10.3389\/fonc.2018.00364","article-title":"Multiple Roles of Glycans in Hematological Malignancies","volume":"8","author":"Pang","year":"2018","journal-title":"Front. Oncol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1146\/annurev-pathol-012414-040438","article-title":"Protein glycosylation in cancer","volume":"10","author":"Stowell","year":"2015","journal-title":"Annu. Rev. Pathol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1093\/glycob\/cwp065","article-title":"Targeted glycoproteomic identification of cancer cell glycosylation","volume":"19","author":"Powlesland","year":"2009","journal-title":"Glycobiology"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1007\/s00280-008-0825-4","article-title":"Growth inhibitory activity of a novel lectin from Cliona varians against K562 human erythroleukemia cells","volume":"63","author":"Queiroz","year":"2009","journal-title":"Cancer Chemother. Pharmacol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1007\/s10930-011-9356-7","article-title":"Cytotoxicity and glycan-binding profile of a D-galactose-binding lectin from the eggs of a Japanese sea hare (Aplysia kurodai)","volume":"30","author":"Kawsar","year":"2011","journal-title":"Protein J."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1016\/j.ijbiomac.2017.06.074","article-title":"Lectin CGL from the sea mussel Crenomytilus grayanus induces Burkitt\u2019s lymphoma cells death via interaction with surface glycan","volume":"104","author":"Chernikov","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"26896","DOI":"10.18632\/oncotarget.15849","article-title":"Fungal lectin MpL enables entry of protein drugs into cancer cells and their subcellular targeting","volume":"8","author":"Zurga","year":"2017","journal-title":"Oncotarget"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/s10930-011-9369-2","article-title":"MRP1 expressed on Burkitt\u2019s lymphoma cells was depleted by catfish egg lectin through Gb3-glycosphingolipid and enhanced cytotoxic effect of drugs","volume":"31","author":"Fujii","year":"2012","journal-title":"Protein J."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.cbpa.2006.08.028","article-title":"CvL, a lectin from the marine sponge Cliona varians: Isolation, characterization and its effects on pathogenic bacteria and Leishmania promastigotes","volume":"145","author":"Moura","year":"2006","journal-title":"Comp. Biochem. Physiol. A Mol. Integr. Physiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"32810","DOI":"10.1074\/jbc.M304116200","article-title":"Emergence and disappearance of an immune molecule, an antimicrobial lectin, in basal metazoa. A tachylectin-related protein in the sponge Suberitesdomuncula","volume":"278","author":"Schroder","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_17","first-page":"133","article-title":"Lipopolysaccharide inner core oligosaccharide structure and outer membrane stability in human pathogens belonging to the Enterobacteriaceae","volume":"11","author":"Frirdich","year":"2005","journal-title":"J. Endotoxin Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"4169","DOI":"10.1046\/j.1432-1033.2002.03131.x","article-title":"Identification and localization of glycine in the inner core lipopolysaccharide of Neisseria meningitidis","volume":"269","author":"Cox","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"647352","DOI":"10.1100\/2012\/647352","article-title":"The chemical composition of endotoxin isolated from intestinal strain of Desulfovibrio desulfuricans","volume":"2012","author":"Lodowska","year":"2012","journal-title":"Sci. World J."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"255","DOI":"10.2331\/suisan.47.255","article-title":"A natural agglutinin inhibitable by d-galacturonic acid in the sea hare Aplysia eggs: Characterization and purification","volume":"47","author":"Kamiya","year":"1981","journal-title":"Nippon. Suisan Gakk."},{"key":"ref_21","first-page":"709","article-title":"Purification and biochemical characterization of D-galactose binding lectin from Japanese sea hare (Aplysia kurodai) eggs","volume":"74","author":"Kawsar","year":"2009","journal-title":"Biochemistry"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"13990","DOI":"10.3390\/molecules190913990","article-title":"A galactose-binding lectin isolated from Aplysia kurodai (sea hare) eggs inhibits streptolysin-induced hemolysis","volume":"19","author":"Hasan","year":"2014","journal-title":"Molecules"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/0014-5793(85)80273-8","article-title":"Purification and characterization of the gonad lectin of Aplysia depilans","volume":"181","author":"Susswein","year":"1985","journal-title":"FEBS Lett."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/s10126-017-9728-x","article-title":"Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial\/antibiofilm potential","volume":"19","author":"Carneiro","year":"2017","journal-title":"Mar. Biotechnol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1002\/neu.480230611","article-title":"Modulation of growth of Aplysia neurons by an endogenous lectin","volume":"23","author":"Wilson","year":"1992","journal-title":"J. Neurobiol."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Motohashi, S., Jimbo, M., Naito, T., Suzuki, T., Sakai, R., and Kamiya, H. (2017). Isolation, amino acid sequences, and plausible functions of the galacturonic acid-binding egg lectin of the Sea hare Aplysia kurodai. Mar. Drugs., 15.","DOI":"10.3390\/md15060161"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1016\/j.ijbiomac.2018.11.170","article-title":"Characterization and assessment of antioxidant and antibacterial activities of sulfated polysaccharides extracted from cuttlefish skin and muscle","volume":"123","author":"Jridi","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.2298\/ABS1004027K","article-title":"The cytotoxic activity of two D-galactose-binding lectins purified from marine invertebrates","volume":"62","author":"Kawsar","year":"2010","journal-title":"Arch. Biol. Sci."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Hasan, I., Asaduzzaman, A.K.M., Swarna, R.R., Fujii, Y., Ozeki, Y., Uddin, M.B., and Kabir, S.R. (2019). MytiLec-1 shows glycan-dependent toxicity against brine shrimp Artemia and induces apoptotic death of Ehrlich ascites carcinoma cells in vivo. Mar Drugs., 17.","DOI":"10.3390\/md17090502"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1590\/0001-3765201520140399","article-title":"Hemagglutinating\/Hemolytic activities in extracts of marine invertebrates from the Brazilian coast and isolation of two lectins from the marine sponge Cliona varians and the sea cucumber Holothuria grisea","volume":"87","author":"Moura","year":"2015","journal-title":"An. Acad. Bras. Cienc."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1002\/jmr.2243","article-title":"Halilectin 1 (H-1) and Halilectin 2 (H-2): Two new lectins isolated from the marine sponge Haliclona caerulea","volume":"26","author":"Carneiro","year":"2013","journal-title":"J. Mol. Recognit."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"3169","DOI":"10.3892\/ol.2017.6484","article-title":"Anticancer activity and antioxidant potential of Aponogeton undulatus against Ehrlich ascites carcinoma cells in Swiss albino mice","volume":"14","author":"Rahman","year":"2017","journal-title":"Oncol. Lett."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"5280","DOI":"10.1021\/bi00292a006","article-title":"Occurrence of alpha-D-galactosyl-containing glycoproteins on Ehrlich tumor cell membranes","volume":"22","author":"Eckhardt","year":"1983","journal-title":"Biochemistry"},{"key":"ref_34","first-page":"1347","article-title":"Egg lectin of Rana japonica and its receptor glycoprotein of Ehrlich tumor cells","volume":"39","author":"Sakakibara","year":"1979","journal-title":"Cancer Res."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"727","DOI":"10.3390\/md10040727","article-title":"A lactose-binding lectin from the marine sponge Cinachyrellaapion (Cal) induces cell death in human cervical adenocarcinoma cells","volume":"10","author":"Rabelo","year":"2012","journal-title":"Mar. Drugs."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1016\/j.ijbiomac.2017.09.116","article-title":"Structural characterization of two isolectins from the marine red alga Solieria filiformis (K\u00fctzing) P.W. Gabrielson and their anticancer effect on MCF-7 breast cancer cells","volume":"107","author":"Chaves","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"4505","DOI":"10.1038\/srep04505","article-title":"Exogenous expression of marine lectins DlFBL and SpRBL induces cancer cell apoptosis possibly through PRMT5-E2F-1 pathway","volume":"4","author":"Wu","year":"2014","journal-title":"Sci. Rep."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"4327","DOI":"10.1007\/s00018-015-2008-x","article-title":"Towards molecular mechanisms regulating the expression of galectins in cancer cells under microenvironmental stress conditions","volume":"72","author":"Timoshenko","year":"2015","journal-title":"Cell Mol. Life Sci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1007\/s10719-012-9379-0","article-title":"Galectins and their ligands: Negative regulators of anti-tumor immunity","volume":"29","author":"Dimitroff","year":"2012","journal-title":"Glycoconj. J."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Verhoeckx, K., Cotter, P., Lopez-Exposito, I., Kleiveland, C., Lea, T., Mackie, A., Requena, T., Swiatecka, D., and Wichers, H. (2015). THP-1 and U937 Cells. The Impact of Food Bioactives on Health, Springer International Publishing. [1st ed.].","DOI":"10.1007\/978-3-319-16104-4"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1271\/bbb.63.341","article-title":"Involvement of N-acetylcysteine-sensitive pathways in ricin-induced apoptotic cell death in U937 cells","volume":"63","author":"Oda","year":"1999","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1271\/bbb.64.1422","article-title":"Isolated ricin B-chain-mediated apoptosis in U937 cells","volume":"64","author":"Hasegawa","year":"2000","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1128\/IAI.00910-07","article-title":"Recognition of bacterial surface polysaccharides by lectins of the innate immune system and its contribution to defense against Infection: The case of pulmonary pathogens","volume":"76","author":"Sahly","year":"2008","journal-title":"Infect. Immun."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Hasan, I., Gerdol, M., Fujii, Y., Rajia, S., Koide, Y., Yamamoto, D., Kawsar, S.M., and Ozeki, Y. (2016). cDNA and gene structure of MytiLec-1, a bacteriostatic R-type lectin from the mediterranean mussel (Mytilus galloprovincialis). Mar Drugs., 14.","DOI":"10.3390\/md14050092"},{"key":"ref_45","first-page":"82","article-title":"Growth inhibitory effects on microorganisms by a D-galactose-binding lectin purified from the sea hare (Aplysia kurodai) eggs: An in vitro study","volume":"8","author":"Kawsar","year":"2010","journal-title":"Nat. Sci."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.gene.2013.08.042","article-title":"A C-type lectin (AiCTL-3) from bay scallop Argopecten irradians with mannose\/galactose binding ability to bind various bacteria","volume":"531","author":"Huang","year":"2013","journal-title":"Gene"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3755","DOI":"10.1007\/s00253-015-6518-0","article-title":"Marine lectins and their medicinal applications","volume":"99","author":"Cheung","year":"2015","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1139\/m89-054","article-title":"Ultrastructural study of galacturonic acid distribution in some pathogenic fungi using gold-complexed Aplysia depilans gonad lectin","volume":"35","author":"Benhamou","year":"1989","journal-title":"Can. J. Microbiol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1007\/BF00403225","article-title":"Cell wall polysaccharides from Talaromyces species","volume":"146","author":"Ruperez","year":"1986","journal-title":"Arch. Microbiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/0145-305X(94)00055-K","article-title":"Antifungal activity of Aplysianin E, a cytotoxic protein of sea hare (Aplysia kurodai) eggs","volume":"19","author":"Iijima","year":"1995","journal-title":"Dev. Comp. Immunol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/j.fsi.2014.11.036","article-title":"A lectin with antifungal activity from the mussel Crenomytilus grayanus","volume":"42","author":"Chikalovets","year":"2015","journal-title":"Fish Shellfish Immunol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1590\/S1517-83822012000200042","article-title":"Antifungal activity of lectins against yeast of vaginal secretion","volume":"43","author":"Gomes","year":"2012","journal-title":"Braz. J. Microbiol."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Ituarte, S., Brola, T.R., Fernandez, P.E., Mu, H., Qiu, J.-W., Heras, H., and Dreon, M.S. (2018). A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0198361"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2391","DOI":"10.1021\/bi00223a014","article-title":"Amino acid sequence and molecular characterization of a D-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs","volume":"30","author":"Ozeki","year":"1991","journal-title":"Biochemistry"},{"key":"ref_56","unstructured":"Finney, D.J. (1971). Probit Analysis, Cambridge University Press. [3rd ed.]."}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/19\/7\/394\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:30:17Z","timestamp":1760164217000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/19\/7\/394"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7,14]]},"references-count":56,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2021,7]]}},"alternative-id":["md19070394"],"URL":"https:\/\/doi.org\/10.3390\/md19070394","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,7,14]]}}}