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 journalArticle

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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

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Arthropod Proteins
Complement Factor D
Horseshoe Crabs
Hemocytes
Serine Proteases
Sequence Homology
Proteins
Catalytic Domain
Interleukin-6 Receptors
Amino Acids
Plasminogen
Tissue Plasminogen Activator
Protein Sorting Signals
Gram-Negative Bacteria
Gene Library
Open Reading Frames
Amino Acid Sequence
Glycoproteins
Bacteria
Screening

All Science Journal Classification (ASJC) codes

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

Cite this

Limulus factor D, a 43-kDa protein isolated from horseshoe crab hemocytes, is a serine protease homologue with antimicrobial activity. / Kawabata, Shun-Ichiro; Tokunaga, Fuminori; Kugi, Yoshie; Motoyama, Shiho; Miura, Yoshiki; Hirata, Michimasa; Iwanaga, Sadaaki.

In: FEBS Letters, Vol. 398, No. 2-3, 02.12.1996, p. 146-150.

Research output: Contribution to journalArticle

Kawabata, Shun-Ichiro ; Tokunaga, Fuminori ; Kugi, Yoshie ; Motoyama, Shiho ; Miura, Yoshiki ; Hirata, Michimasa ; Iwanaga, Sadaaki. / Limulus factor D, a 43-kDa protein isolated from horseshoe crab hemocytes, is a serine protease homologue with antimicrobial activity. In: FEBS Letters. 1996 ; Vol. 398, No. 2-3. pp. 146-150.
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AU - Hirata, Michimasa

AU - Iwanaga, Sadaaki

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