Comprehensive sequence analysis of horseshoe crab cuticular proteins and their involvement in transglutaminase-dependent cross-linking

Manabu Iijima, Tomonori Hashimoto, Yasuyuki Matsuda, Taku Nagai, Yuichiro Yamano, Tomohiko Ichi, Tsukasa Osaki, Shun-Ichiro Kawabata

研究成果: ジャーナルへの寄稿記事

31 引用 (Scopus)

抄録

Arthropod cuticles play an important role as the first barrier against invading pathogens. We extensively determined the sequences of horseshoe crab cuticular proteins. Proteins extracted from a part of the ventral side of the cuticle were purified by chitin-affinity chromatography, and separated by two-dimensional SDS/PAGE. Proteins appearing on the gel were designated high molecular mass chitin-binding proteins, and these proteins were then grouped into classes based on their approximate isoelectric points and predominant amino acid compositions. Members of groups designated basic G, basic Y, and acidic S groups contained a so-called Rebers and Riddiford consensus found in arthropod cuticular proteins. Proteins designated acidic DE25 and DE29 each contained a Cys-rich domain with sequences similar to those of insect peritrophic matrix proteins and chitinases. In contrast, basic QH4 and QH10 contained no consensus sequences found in known chitin-binding proteins. Alternatively, a low molecular mass chitin-binding fraction was prepared by size exclusion chromatography, and 15 low molecular mass chitin-binding proteins, named P1 through P15, were isolated. With the exception of P9 and P15, all were found to be identical to known antimicrobial peptides. P9 consisted of a Kunitz-type chymotrypsin inhibitor sequence, and P15 contained a Cys-rich motif found in insulin-like growth factor-binding proteins. Interestingly, we observed transglutaminase- dependent polymerization of nearly all high molecular mass chitin-binding proteins, a finding suggests that transglutaminase-dependent cross-linking plays an important role in host defense in the arthropod cuticle, analogous to that observed in the epidermal cornified cell envelope in mammals.

元の言語英語
ページ(範囲)4774-4786
ページ数13
ジャーナルFEBS Journal
272
発行部数18
DOI
出版物ステータス出版済み - 9 1 2005

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Arthropod Proteins
Transglutaminases
Chitin
Sequence Analysis
Molecular mass
Carrier Proteins
Proteins
Arthropods
Chitinases
Insulin-Like Growth Factor Binding Proteins
Affinity chromatography
Consensus Sequence
Isoelectric Point
Chymotrypsin
Mammals
Size exclusion chromatography
Affinity Chromatography
Polymerization
Pathogens
Gel Chromatography

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Comprehensive sequence analysis of horseshoe crab cuticular proteins and their involvement in transglutaminase-dependent cross-linking. / Iijima, Manabu; Hashimoto, Tomonori; Matsuda, Yasuyuki; Nagai, Taku; Yamano, Yuichiro; Ichi, Tomohiko; Osaki, Tsukasa; Kawabata, Shun-Ichiro.

:: FEBS Journal, 巻 272, 番号 18, 01.09.2005, p. 4774-4786.

研究成果: ジャーナルへの寄稿記事

Iijima, Manabu ; Hashimoto, Tomonori ; Matsuda, Yasuyuki ; Nagai, Taku ; Yamano, Yuichiro ; Ichi, Tomohiko ; Osaki, Tsukasa ; Kawabata, Shun-Ichiro. / Comprehensive sequence analysis of horseshoe crab cuticular proteins and their involvement in transglutaminase-dependent cross-linking. :: FEBS Journal. 2005 ; 巻 272, 番号 18. pp. 4774-4786.
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