Halilectin 1 (H‐1) and Halilectin 2 (H‐2): two new lectins isolated from the marine sponge Haliclona caerulea. Issue 1 (11th December 2012)

• Record Type: Journal Article
• Authors: Carneiro, Rômulo Farias; de, Arthur Alves; Nascimento, Fernando Edson Pessoa do; Simplicio, Clareane Avelino; Nascimento, Kyria Santiago do; Rocha, Bruno Anderson Matias da; Saker‐Sampaio, Silvana; Moura, Raniere da Mata; Mota, Sula Salani; Cavada, Benildo Sousa; Nagano, Celso Shiniti; Sampaio, Alexandre Holanda
• Is Part Of: Journal of molecular recognition. Volume 26:Issue 1(2013:Jan.)
• Page Start: 51
• Page End: 58
• Publication Date: 2012-12-11
• Subjects: Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2243
• Languages: English
• ISSNs: 0952-3499

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Two new lectins named Halilectin 1 (H‐1) and Halilectin 2 (H‐2) were isolated from the marine sponge <italic>Haliclona caerulea</italic> using a combination of affinity chromatography on stroma fixed onto Sephadex G‐25 and cation and anion exchange chromatography. H‐1 is a monomeric protein with a molecular mass of 40 kDa estimated using sodium dodecyl sulfate polyacrylamide gel electrophoresis and 15 kDa estimated using a TSK gel. Conversely, H‐2 is a homodimeric protein with 15 kDa monomers linked via weak interactions. H‐1 more effectively agglutinates trypsinized rabbit erythrocytes, whereas H‐2 more effectively agglutinates native rabbit erythrocytes. The hemagglutinating activity of H‐1 could be not inhibited by any tested sugars, but H‐2 was inhibited by orosomucoid and porcine stomach mucin. Neither lectin was dependent on divalent ions. H‐1 was stable at basic pH range and temperatures up to 50 °C, whereas H‐2 was stable at acid pH range and temperatures up to 80 °C. The <italic>H. caerulea</italic> lectins exhibited dose‐dependent toxicity against <italic>Artemia</italic> nauplii. Additionally, 76% of the primary structure of H‐2 was determined using tandem mass spectrometry to contain a unique amino acid sequence with no similarity to any members of the animal lectin family. Copyright © 2012 John Wiley &amp; Sons, Ltd.</p> </abstract>