Limulus factor D, a 43-kDa protein isolated from horseshoe crab hemocytes, is a serine protease homologue with antimicrobial activity

Shun Ichiro Kawabata, Fuminori Tokunaga, Yoshie Kugi, Shiho Motoyama, Yoshiki Miura, Michimasa Hirata, Sadaaki Iwanaga

Research output: Contribution to journalArticlepeer-review

62 Citations (Scopus)

Abstract

A glycoprotein (M(r) = 43000) from horseshoe crab hemocytes with antimicrobial activity against Gram-negative bacteria was purified. The internal peptide sequences coincided exactly with the deduced amino acid sequence of a cDNA clone, designated limulus factor D, which was isolated by screening a hemocyte cDNA library with an anti-human plasminogen antibody. The open reading frame codes for a precursor of factor D of 394 amino acid residues, including an NH2-terminal signal sequence. The COOH-terminal domain of factor D has significant sequence homology with the catalytic domain of mammalian serine proteases, in particular with human tissue plasminogen activator (32% identity), except for the substitution of Ser of the active site triad to Gly. Factor D has a unique NH2-terminal domain with weak sequence homology with part of the mammalian interleukin-6 receptor α-chain. Factor D is likely to have an important role in host defense mechanisms.

Original languageEnglish
Pages (from-to)146-150
Number of pages5
JournalFEBS Letters
Volume398
Issue number2-3
DOIs
Publication statusPublished - Dec 2 1996

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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