TY - JOUR
T1 - Limulus factor D, a 43-kDa protein isolated from horseshoe crab hemocytes, is a serine protease homologue with antimicrobial activity
AU - Kawabata, Shun Ichiro
AU - Tokunaga, Fuminori
AU - Kugi, Yoshie
AU - Motoyama, Shiho
AU - Miura, Yoshiki
AU - Hirata, Michimasa
AU - Iwanaga, Sadaaki
N1 - Funding Information:
Acknowledgements: We thank C. Yano for excellent technical assistance in amino acid and sequence analyses and S. Matsumura for secretarial services. M. Ohara provided helpful comments on the manuscript. This work was supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan.
PY - 1996/12/2
Y1 - 1996/12/2
N2 - 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.
AB - 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.
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U2 - 10.1016/S0014-5793(96)01224-0
DO - 10.1016/S0014-5793(96)01224-0
M3 - Article
C2 - 8977095
AN - SCOPUS:0030566866
SN - 0014-5793
VL - 398
SP - 146
EP - 150
JO - FEBS Letters
JF - FEBS Letters
IS - 2-3
ER -