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A more recent version of this article appeared on February 9, 2007
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M609198200v1
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Papers In Press, published online ahead of print November 29, 2006
J. Biol. Chem, 10.1074/jbc.M609198200
Submitted on September 28, 2006
Revised on November 15, 2006
Accepted on November 29, 2006

A structural perspective on the interaction between lipopolysaccharide and factor C, a receptor involved in recognition of Gram-negative bacteria

Takumi Koshiba, Tomoyuki Hashii, and Shun-ichiro Kawabata

Department of Biology, Kyushu University, Fukuoka 812-8581

Corresponding Author: skawascb{at}mbox.nc.kyushu-u.ac.jp

The recognition of broadly conserved microorganism components, known as pathogen-associated molecular patterns, is an essential step in initiating the innate immune response. In the horseshoe crab, stimulation of hemocytes with lipopolysaccharide (LPS) causes the activation of its innate immune response, and Factor C, a serine protease zymogen, plays an important role in this event. Here, we report that Factor C associates with LPS on the hemocyte surface and directly recognizes Gram-negative bacteria. Structure-function analyses reveal that the LPS-binding site is present in the amino-terminal cysteine-rich (Cys-rich) region of the molecule, and that it contains a tri-peptide sequence consisting of an aromatic residue flanked by two basic residues, that is conserved in other mammalian LPS-recognizing proteins. Moreover, we demonstrate that the Cys-rich region specifically binds to LPS on Gram-negative bacteria, and that mutations in the tri-peptide motif abrogate its association with both LPS and Gram-negative bacteria, underscoring the importance of the tri-peptide in LPS interaction. Although the innate immune response to LPS in the horseshoe crab is distinct from that of mammals, it appears to rely on structural features that are conserved among LPS-recognizing proteins from diverse species.


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