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<p>The complement system, a key humoral component of innate immunity, plays a critical role in the defense of fish. However, many aspects of its reaction mechanisms remain unclear in fish due to a lack of functional analyses at the protein level. Complement component C5 contributes to host protection by forming the membrane attack complex (MAC), which directly lyses pathogens, and by mediating inflammatory responses. We previously identified two divergent C5 isotypes (C5-I and C5-II) in the common carp, but their functional differences at the protein level have not been established. In this study, we expressed the netrin domain of carp C5-I as a recombinant protein in prokaryotic cells and used it to generate a specific antibody. Using this antibody, we demonstrated that C5-I is the predominant C5 isoform in carp serum under basal, uninfected conditions and that it participates in MAC formation. In addition, we developed a rapid, small-scale purification method for functionally active carp C5-I using immunoaffinity chromatography with an anti-C5-I–immobilized column.</p>

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Identification of C5-I as a functionally dominant isotype of the complement component C5 in the common carp Cyprinus carpio

  • 期刊论文

  • 发表日期：

    2026年3月7日

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  • Michiyo Kimura,
  • Takahiro Nagasawa,
  • Tomonori Somamoto,
  • Miki Nakao

摘要

The complement system, a key humoral component of innate immunity, plays a critical role in the defense of fish. However, many aspects of its reaction mechanisms remain unclear in fish due to a lack of functional analyses at the protein level. Complement component C5 contributes to host protection by forming the membrane attack complex (MAC), which directly lyses pathogens, and by mediating inflammatory responses. We previously identified two divergent C5 isotypes (C5-I and C5-II) in the common carp, but their functional differences at the protein level have not been established. In this study, we expressed the netrin domain of carp C5-I as a recombinant protein in prokaryotic cells and used it to generate a specific antibody. Using this antibody, we demonstrated that C5-I is the predominant C5 isoform in carp serum under basal, uninfected conditions and that it participates in MAC formation. In addition, we developed a rapid, small-scale purification method for functionally active carp C5-I using immunoaffinity chromatography with an anti-C5-I–immobilized column.