Next Article in Journal
Cyanobacterial Toxins of the Laurentian Great Lakes, Their Toxicological Effects, and Numerical Limits in Drinking Water
Next Article in Special Issue
A Novel High-Mannose Specific Lectin from the Green Alga Halimeda renschii Exhibits a Potent Anti-Influenza Virus Activity through High-Affinity Binding to the Viral Hemagglutinin
Previous Article in Journal
The Rising Tide of Antimicrobial Resistance in Aquaculture: Sources, Sinks and Solutions
Previous Article in Special Issue
Marine Lectins DlFBL and HddSBL Fused with Soluble Coxsackie-Adenovirus Receptor Facilitate Adenovirus Infection in Cancer Cells BUT Have Different Effects on Cell Survival
Article Menu
Issue 6 (June) cover image

Export Article

Open AccessArticle
Mar. Drugs 2017, 15(6), 161;

Isolation, Amino Acid Sequences, and Plausible Functions of the Galacturonic Acid-Binding Egg Lectin of the Sea Hare Aplysia kurodai

Department of Marine Biosciences, School of Marine Biosciences, Kitasato University,1-15-1, Minami-ku, Kitasato, Sagamihara, Kanagawa 252-0373, Japan
Faculty of Fisheries Sciences, Hokkaido University, Hakodate 041-8611, Japan
Author to whom correspondence should be addressed.
Received: 31 March 2017 / Revised: 12 May 2017 / Accepted: 25 May 2017 / Published: 2 June 2017
(This article belongs to the Special Issue Structures, Functions and Applications of Marine Lectins)
Full-Text   |   PDF [3337 KB, uploaded 5 June 2017]   |  


Egg lectins occur in a variety of animals ranging from mollusks to vertebrates. A few examples of molluscan egg lectins have been reported, including that of the sea hare Aplysia kurodai; however, their biological functions in the egg remain unclarified. We report the isolation, determination of primary structure, and possible functions of A. kurodai lectin (AKL) from the egg mass of A. kurodai. We obtained AKL as an inseparable mixture of isoproteins with a relative molecular mass of approximately 32 kDa by affinity purification. The hemagglutinating activity of AKL against rabbit erythrocytes was inhibited most potently by galacturonic acid and moderately by xylose. Nucleotide sequencing of corresponding cDNA obtained by rapid amplification of cDNA ends (RACE) allowed us to deduce complete amino acid sequences. The mature polypeptides consisted of 218- or 219-amino acids with three repeated domains. The amino acid sequence had similarities to hypothetical proteins of Aplysia spp., or domain DUF3011 of uncharacterized bacterial proteins. AKL is the first member of the DUF3011 family whose function, carbohydrate recognition, was revealed. Treatment of the egg with galacturonic acid, an AKL sugar inhibitor, resulted in deformation of the veliger larvae, suggesting that AKL is involved in organogenesis in the developmental stage of A. kurodai. View Full-Text
Keywords: Aplysia kurodai; egg lectin; embryonic development; galacturonic acid Aplysia kurodai; egg lectin; embryonic development; galacturonic acid

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Motohashi, S.; Jimbo, M.; Naito, T.; Suzuki, T.; Sakai, R.; Kamiya, H. Isolation, Amino Acid Sequences, and Plausible Functions of the Galacturonic Acid-Binding Egg Lectin of the Sea Hare Aplysia kurodai. Mar. Drugs 2017, 15, 161.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top