Scholarlink

<p>A screening of 29 Palauan marine sponge extracts via stepwise screening techniques, including hemagglutination, cytotoxicity, and cell-internalization assays, resulted in the discovery of a potent cytotoxic lectin, RaspL, isolated from a marine sponge <i>Aulospongus</i> sp. (family Raspailiidae). RaspL consists of ~14&#xa0;kDa protomers forming approximately 100&#xa0;kDa oligomers. Partial de novo amino acid sequence analysis revealed a peptide contig of 38 residues with no sequence similarity to other reported proteins. RaspL agglutinated rabbit erythrocytes at a minimum concentration of 146&#xa0;ng/mL, with hemagglutination specifically inhibited by N-acetylated sugars, including GalNAc, NANA, and GlcNAc, with minimum inhibitory concentrations of 4.2, 16.7, and 33.3&#xa0;mM<span>,</span> respectively. RaspL remained bioactive across pH 3.0–12.0 and temperatures up to 100&#xa0;°C for 90&#xa0;min. It showed potent cytotoxicity against HeLa cells (IC<sub>50</sub> of 4.36&#xa0;µg/mL), comparable to a cytotoxic legume lectin, Concanavalin A (IC<sub>50</sub> of 19.08&#xa0;µg/mL). Confocal microscopic observation confirmed its cellular internalization and Golgi localization. The potent cytotoxicity, sugar-binding specificity, physicochemical stability, and Golgi targeting underscore RaspL as a unique candidate for further exploration in biomedical research, particularly in cancer cell biology and glycobiology.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

RaspL: isolation and characterization of a cell-invading, cytotoxic lectin from the Palauan marine sponge

  • 期刊论文

  • 发表日期：

    2025年12月18日

查看全文
  • Syeda Sobia Nasir,
  • Yuji Sawada,
  • Yoshikazu Tanaka,
  • Yuji Ise,
  • Hiromi Watari,
  • Ryuichi Sakai

摘要

A screening of 29 Palauan marine sponge extracts via stepwise screening techniques, including hemagglutination, cytotoxicity, and cell-internalization assays, resulted in the discovery of a potent cytotoxic lectin, RaspL, isolated from a marine sponge Aulospongus sp. (family Raspailiidae). RaspL consists of ~14 kDa protomers forming approximately 100 kDa oligomers. Partial de novo amino acid sequence analysis revealed a peptide contig of 38 residues with no sequence similarity to other reported proteins. RaspL agglutinated rabbit erythrocytes at a minimum concentration of 146 ng/mL, with hemagglutination specifically inhibited by N-acetylated sugars, including GalNAc, NANA, and GlcNAc, with minimum inhibitory concentrations of 4.2, 16.7, and 33.3 mM, respectively. RaspL remained bioactive across pH 3.0–12.0 and temperatures up to 100 °C for 90 min. It showed potent cytotoxicity against HeLa cells (IC50 of 4.36 µg/mL), comparable to a cytotoxic legume lectin, Concanavalin A (IC50 of 19.08 µg/mL). Confocal microscopic observation confirmed its cellular internalization and Golgi localization. The potent cytotoxicity, sugar-binding specificity, physicochemical stability, and Golgi targeting underscore RaspL as a unique candidate for further exploration in biomedical research, particularly in cancer cell biology and glycobiology.