Wheat germ agglutinin affinity chromatography enrichment and glyco-proteomic characterization of tetrodotoxin-binding proteins from the plasma of cultured tiger pufferfish (<i>Takifugu rubripes</i>)-Reference-Cited by-同舟云学术

Wheat germ agglutinin affinity chromatography enrichment and glyco-proteomic characterization of tetrodotoxin-binding proteins from the plasma of cultured tiger pufferfish (Takifugu rubripes)

Published:2023-07-17 Issue:10 Volume:87 Page:1155-1168
ISSN:1347-6947
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Zhang Yafei¹,Minami Ryoma¹²,Tatsuno Ryohei³,Gao Wei¹⁴,Ueno Mikinori¹,Yamada Akinori¹,Yoshida Asami¹,Sedanza Mary Grace⁵,Arima Kazunari⁶,Takatani Tomohiro¹,Yamaguchi Kenichi¹,Oshima Yuji⁷,Arakawa Osamu¹

Affiliation:

1. Graduate School of Fisheries and Environmental Sciences, Nagasaki University , Bunkyo-machi, Nagasaki , Japan

2. Division of Transcriptomics, Medical Institute of Bioregulation, Kyushu University , Maidashi, Higashi-ku, Fukuoka , Japan

3. National Fisheries University , Japan Fisheries Research and Education Agency, Nagatahonmachi, Shimonoseki, Yamaguchi , Japan

4. Dalian Blue Peptide Technology Research & Development Co. , Ltd, Dalian , China

5. Institute of Aquaculture, College of Fisheries and Ocean Sciences, University of the Philippines Visayas , Miagao, Iloilo, Philippines

6. Department of Chemistry, Graduate School of Science and Engineering, Kagoshima University , Korimoto, Kagoshima , Japan

7. Laboratory of Marine Environmental Science, Faculty of Agriculture, Kyushu University , Hakozaki, Fukuoka , Japan

Abstract

ABSTRACT Efficient enrichment of tetrodotoxin (TTX)-binding proteins from the plasma of cultured tiger pufferfish (Takifugu rubripes) was achieved by ammonium sulfate fractionation and wheat germ agglutinin (WGA) affinity chromatography. The enrichment efficiency was validated by ultrafiltration-LC/MS-based TTX-binding assay and proteomics. Major proteins in the WGA-bound fraction were identified as isoform X1 (125 kDa) and X2 variants (88 and 79 kDa) derived from pufferfish saxitoxin and tetrodotoxin-binding protein (PSTBP) 1-like gene (LOC101075943). The 125-kDa X1 protein was found to be a novel member of the lipocalin family, having three tandemly repeated domains. X2 variants, X2α and X2β, were estimated to have two domains, and X2β is structurally related to Takifugu pardalis PSTBP2 in their domain type and arrangement. Among 11 potential N-glycosylation sites in the X2 precursor, 5 N-glycosylated Asn residues (N55, N89, N244, N308, and N449) were empirically determined. Structural relationships among PSTBP homologs and complexity of their proteoforms are discussed.

Funder

Japan Society for the Promotion of Science

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

https://academic.oup.com/bbb/advance-article-pdf/doi/10.1093/bbb/zbad095/50984742/zbad095.pdf

Reference63 articles.

1. Effects of N-glycosylation on the folding and structure of plant proteins;Aldo;J Exp Bot,1998

2. The human plasma proteome history, character, and diagnostic prospects;Anderson;Mol Cell Proteomics,2002

3. Concanavalin A interactions with asparagine-linked glycopeptides bivalency of bisected complex type oligosaccharides;Bhattacharyya;J Biol Chem,1987

4. The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid;Bhavanandan;J Biol Chem,1979

5. Odorant and pheromone binding by aphrodisin, a hamster aphrodisiac protein;Briand;FEBS Lett,2000