Novel Galectins Purified from the Sponge Chondrilla australiensis: Unique Structural Features and Cytotoxic Effects on Colorectal Cancer Cells Mediated by TF-Antigen Binding

We here report the purification of a novel member of the galectin family, the β-galactoside-binding lectin hRTL, from the marine sponge <i>Chondrilla australiensis</i>. The hRTL lectin is a tetrameric proto-type galectin with a subunit molecular weight of 15.5 kDa, consisting of 141 amino acids and sharing 92% primary sequence identity with the galectin CCL from the congeneric species <i>C. caribensis</i>. Transcriptome analysis allowed for the identification of additional sequences belonging to the same family, bringing the total number of hRTLs to six. Unlike most other galectins, hRTLs display a 23 amino acid-long signal peptide that, according to Erdman degradation, is post-translationally cleaved, leaving an N-terminal end devoid of acetylated modifications, unlike most other galectins. Moreover, two hRTLs display an internal insertion, which determines the presence of an unusual loop region that may have important functional implications. The characterization of the glycan-binding properties of hRTL revealed that it had high affinity towards TF-antigen, sialyl TF, and type-1 N-acetyl lactosamine with a Galβ1-3 structure. When administered to DLD-1 cells, a colorectal carcinoma cell line expressing mucin-associated TF-antigen, hRTL could induce glycan-dependent cytotoxicity.

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Publication Details

Journal
Marine Drugs
Published
2024-08-31
DOI
https://doi.org/10.3390/md22090400
Citations
3
Primary Topic
Galectins and Cancer Biology
Type
article
Field-Weighted Citation Impact
0.72

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article

Novel Galectins Purified from the Sponge Chondrilla australiensis: Unique Structural Features and Cytotoxic Effects on Colorectal Cancer Cells Mediated by TF-Antigen Binding

Nanae Kobayashi, Kenichi Kamata, Marco Gerdol, Imtiaj Hasan et al.
3 citations
Marine Drugs
Galectins and Cancer Biology
0.72
article

Novel Galectins Purified from the Sponge Chondrilla australiensis: Unique Structural Features and Cytotoxic Effects on Colorectal Cancer Cells Mediated by TF-Antigen Binding

Nanae Kobayashi, Kenichi Kamata, Marco Gerdol, Imtiaj Hasan, Yuji Ise, Sarkar M. A. Kawsar, Kayo Hasehira, Tatsuya Kawasaki, Alberto Pallavicini, Somrita Padma, Nobumitsu Miyanishi, Sultana Rajia, Masao Yamada, Yasuhiro Ozeki, Bishnu P. Chatterjee, Ryuhei Hayashi, Yuki Fujii, Takashi Hayashi, Hideaki Fujita, Yukiko Ogawa, Satoshi Furushima, Ryuya Ishiwata, Daisuke Adachi, Riku Chida, Mayuka Ohkawa, Naoko Masuda, Y. Onoda, Yuka Niimi
article en
3 citations

Abstract

We here report the purification of a novel member of the galectin family, the β-galactoside-binding lectin hRTL, from the marine sponge <i>Chondrilla australiensis</i>. The hRTL lectin is a tetrameric proto-type galectin with a subunit molecular weight of 15.5 kDa, consisting of 141 amino acids and sharing 92% primary sequence identity with the galectin CCL from the congeneric species <i>C. caribensis</i>. Transcriptome analysis allowed for the identification of additional sequences belonging to the same family, bringing the total number of hRTLs to six. Unlike most other galectins, hRTLs display a 23 amino acid-long signal peptide that, according to Erdman degradation, is post-translationally cleaved, leaving an N-terminal end devoid of acetylated modifications, unlike most other galectins. Moreover, two hRTLs display an internal insertion, which determines the presence of an unusual loop region that may have important functional implications. The characterization of the glycan-binding properties of hRTL revealed that it had high affinity towards TF-antigen, sialyl TF, and type-1 N-acetyl lactosamine with a Galβ1-3 structure. When administered to DLD-1 cells, a colorectal carcinoma cell line expressing mucin-associated TF-antigen, hRTL could induce glycan-dependent cytotoxicity.

Marine DrugsVol. 22(9)
University of Trieste (IT), Toyo University (JP), Nagasaki International University (JP), Chittaranjan National Cancer Institute (IN), Varendra University (BD), Protein Research Foundation (JP), University of Chittagong (BD), Yokohama City University (JP), University of Rajshahi (BD), KU Leuven (BE)
European Commission, Ministry of Education, Culture, Sports, Science and Technology, Japan Society for the Promotion of Science, Canadian Glycomics Network
Life below water
Openalex Percentile: Top 29%
Galectins and Cancer Biology
0.72
DOIOpen Access PDFOpenAlex
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