Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen

Soutaro Gokudan, Tatsushi Muta, Ryoko Tsuda, Kumiko Koori, Takeshi Kawahara, Noriaki Seki, Yoshimitsu Mizunoe, Sun N. Wai, Sadaaki Iwanaga, Shun Ichiro Kawabata

Research output: Contribution to journalArticle

155 Citations (Scopus)

Abstract

We have characterized and cloned newly isolated lectins from hemolymph plasma of the horseshoe crab Tachypleus tridentatus, which we named tachylectins 5A and 5B (TLs-5). TLs-5 agglutinated all types of human erythrocytes and Gram-positive and Gram-negative bacteria. TLs-5 specifically recognize acetyl group-containing substances including noncarbohydrates; the acetyl group is required and is sufficient for recognition. TLs-5 enhanced the antimicrobial activity of a horseshoe crab-derived big defensin, cDNA sequences of TLs-5 indicated that they consist of a short N-terminal Cys- containing segment and a C-terminal fibrinogen-like domain with the highest sequence identity (51%) to that of mammalian ficolins. TLs-5, however, lack the collagenous domain found in a kind of 'bouquet arrangement' of ficolins and collectins. Electron microscopy revealed that TLs-5 form two- to four- bladed propeller structures. The horseshoe crab is equipped with a unique functional homologue of vertebrate fibrinogen, coagulogen, as the target protein of the clotting cascade. Our observations clearly show that the horseshoe crab has fibrinogen-related molecules in hemolymph plasma and that they function as nonself-recognizing lectins. An ancestor of fibrinogen may have functioned as a nonself-recognizing protein.

Original languageEnglish
Pages (from-to)10086-10091
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number18
DOIs
Publication statusPublished - Aug 31 1999

Fingerprint

Horseshoe Crabs
Lectins
Innate Immunity
Fibrinogen
Hemolymph
Collectins
Defensins
Tachypleus tridentatus TL-5B protein
Tachypleus tridentatus TL-5A protein
Gram-Negative Bacteria
Vertebrates
Electron Microscopy
Proteins
Complementary DNA
Erythrocytes

All Science Journal Classification (ASJC) codes

  • General

Cite this

Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen. / Gokudan, Soutaro; Muta, Tatsushi; Tsuda, Ryoko; Koori, Kumiko; Kawahara, Takeshi; Seki, Noriaki; Mizunoe, Yoshimitsu; Wai, Sun N.; Iwanaga, Sadaaki; Kawabata, Shun Ichiro.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 18, 31.08.1999, p. 10086-10091.

Research output: Contribution to journalArticle

Gokudan, Soutaro ; Muta, Tatsushi ; Tsuda, Ryoko ; Koori, Kumiko ; Kawahara, Takeshi ; Seki, Noriaki ; Mizunoe, Yoshimitsu ; Wai, Sun N. ; Iwanaga, Sadaaki ; Kawabata, Shun Ichiro. / Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen. In: Proceedings of the National Academy of Sciences of the United States of America. 1999 ; Vol. 96, No. 18. pp. 10086-10091.
@article{224b69c98c394689842089d5d721b085,
title = "Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen",
abstract = "We have characterized and cloned newly isolated lectins from hemolymph plasma of the horseshoe crab Tachypleus tridentatus, which we named tachylectins 5A and 5B (TLs-5). TLs-5 agglutinated all types of human erythrocytes and Gram-positive and Gram-negative bacteria. TLs-5 specifically recognize acetyl group-containing substances including noncarbohydrates; the acetyl group is required and is sufficient for recognition. TLs-5 enhanced the antimicrobial activity of a horseshoe crab-derived big defensin, cDNA sequences of TLs-5 indicated that they consist of a short N-terminal Cys- containing segment and a C-terminal fibrinogen-like domain with the highest sequence identity (51{\%}) to that of mammalian ficolins. TLs-5, however, lack the collagenous domain found in a kind of 'bouquet arrangement' of ficolins and collectins. Electron microscopy revealed that TLs-5 form two- to four- bladed propeller structures. The horseshoe crab is equipped with a unique functional homologue of vertebrate fibrinogen, coagulogen, as the target protein of the clotting cascade. Our observations clearly show that the horseshoe crab has fibrinogen-related molecules in hemolymph plasma and that they function as nonself-recognizing lectins. An ancestor of fibrinogen may have functioned as a nonself-recognizing protein.",
author = "Soutaro Gokudan and Tatsushi Muta and Ryoko Tsuda and Kumiko Koori and Takeshi Kawahara and Noriaki Seki and Yoshimitsu Mizunoe and Wai, {Sun N.} and Sadaaki Iwanaga and Kawabata, {Shun Ichiro}",
year = "1999",
month = "8",
day = "31",
doi = "10.1073/pnas.96.18.10086",
language = "English",
volume = "96",
pages = "10086--10091",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "18",

}

TY - JOUR

T1 - Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen

AU - Gokudan, Soutaro

AU - Muta, Tatsushi

AU - Tsuda, Ryoko

AU - Koori, Kumiko

AU - Kawahara, Takeshi

AU - Seki, Noriaki

AU - Mizunoe, Yoshimitsu

AU - Wai, Sun N.

AU - Iwanaga, Sadaaki

AU - Kawabata, Shun Ichiro

PY - 1999/8/31

Y1 - 1999/8/31

N2 - We have characterized and cloned newly isolated lectins from hemolymph plasma of the horseshoe crab Tachypleus tridentatus, which we named tachylectins 5A and 5B (TLs-5). TLs-5 agglutinated all types of human erythrocytes and Gram-positive and Gram-negative bacteria. TLs-5 specifically recognize acetyl group-containing substances including noncarbohydrates; the acetyl group is required and is sufficient for recognition. TLs-5 enhanced the antimicrobial activity of a horseshoe crab-derived big defensin, cDNA sequences of TLs-5 indicated that they consist of a short N-terminal Cys- containing segment and a C-terminal fibrinogen-like domain with the highest sequence identity (51%) to that of mammalian ficolins. TLs-5, however, lack the collagenous domain found in a kind of 'bouquet arrangement' of ficolins and collectins. Electron microscopy revealed that TLs-5 form two- to four- bladed propeller structures. The horseshoe crab is equipped with a unique functional homologue of vertebrate fibrinogen, coagulogen, as the target protein of the clotting cascade. Our observations clearly show that the horseshoe crab has fibrinogen-related molecules in hemolymph plasma and that they function as nonself-recognizing lectins. An ancestor of fibrinogen may have functioned as a nonself-recognizing protein.

AB - We have characterized and cloned newly isolated lectins from hemolymph plasma of the horseshoe crab Tachypleus tridentatus, which we named tachylectins 5A and 5B (TLs-5). TLs-5 agglutinated all types of human erythrocytes and Gram-positive and Gram-negative bacteria. TLs-5 specifically recognize acetyl group-containing substances including noncarbohydrates; the acetyl group is required and is sufficient for recognition. TLs-5 enhanced the antimicrobial activity of a horseshoe crab-derived big defensin, cDNA sequences of TLs-5 indicated that they consist of a short N-terminal Cys- containing segment and a C-terminal fibrinogen-like domain with the highest sequence identity (51%) to that of mammalian ficolins. TLs-5, however, lack the collagenous domain found in a kind of 'bouquet arrangement' of ficolins and collectins. Electron microscopy revealed that TLs-5 form two- to four- bladed propeller structures. The horseshoe crab is equipped with a unique functional homologue of vertebrate fibrinogen, coagulogen, as the target protein of the clotting cascade. Our observations clearly show that the horseshoe crab has fibrinogen-related molecules in hemolymph plasma and that they function as nonself-recognizing lectins. An ancestor of fibrinogen may have functioned as a nonself-recognizing protein.

UR - http://www.scopus.com/inward/record.url?scp=4243869181&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=4243869181&partnerID=8YFLogxK

U2 - 10.1073/pnas.96.18.10086

DO - 10.1073/pnas.96.18.10086

M3 - Article

C2 - 10468566

AN - SCOPUS:4243869181

VL - 96

SP - 10086

EP - 10091

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 18

ER -