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<p><i>Bathynomus doederleini</i> is a deep-sea isopod belonging to the subphylum Crustacea that is frequently captured as bycatch. Although <i>B. doederleini</i> has recently attracted interest as a potential novel marine food resource, its allergenic risk has not been evaluated. Because crustacean-allergic individuals may react to conserved allergens present across crustaceans, we investigated the molecular and immunological properties of <i>B. doederleini</i> proteins. Immunoassays using sera from crustacean-allergic patients with no prior exposure to <i>B. doederleini</i> demonstrated significant immunoglobulin E (IgE) reactivity to the heated extract of <i>B. doederleini</i> and revealed a major IgE-reactive band at approximately 37&#xa0;kDa. Western blotting using an anti-tropomyosin antibody and liquid chromatography–tandem mass spectrometry (LC–MS/MS) analysis identified the 37&#xa0;kDa protein as tropomyosin (TM). The <i>TM</i> cDNA containing the complete open reading frame (ORF) was cloned, revealing a transcript encoding a 284-amino-acid polypeptide sharing 91–98% identity with other crustacean TMs. These findings indicate that <i>B. doederleini</i> possesses a cross-reactive TM capable of triggering IgE binding in unexposed individuals.</p>

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Molecular and immunological characterization of tropomyosin from the deep-sea isopod Bathynomus doederleini

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年5月6日

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  • Kouichi Kurose,
  • Orina Iwakawa–Ozawa,
  • Keiji Kito,
  • Kuniyoshi Shimakura,
  • Kazufumi Osako,
  • Hiroki Koyama

摘要

Bathynomus doederleini is a deep-sea isopod belonging to the subphylum Crustacea that is frequently captured as bycatch. Although B. doederleini has recently attracted interest as a potential novel marine food resource, its allergenic risk has not been evaluated. Because crustacean-allergic individuals may react to conserved allergens present across crustaceans, we investigated the molecular and immunological properties of B. doederleini proteins. Immunoassays using sera from crustacean-allergic patients with no prior exposure to B. doederleini demonstrated significant immunoglobulin E (IgE) reactivity to the heated extract of B. doederleini and revealed a major IgE-reactive band at approximately 37 kDa. Western blotting using an anti-tropomyosin antibody and liquid chromatography–tandem mass spectrometry (LC–MS/MS) analysis identified the 37 kDa protein as tropomyosin (TM). The TM cDNA containing the complete open reading frame (ORF) was cloned, revealing a transcript encoding a 284-amino-acid polypeptide sharing 91–98% identity with other crustacean TMs. These findings indicate that B. doederleini possesses a cross-reactive TM capable of triggering IgE binding in unexposed individuals.