TAILIEUCHUNG - Báo cáo khoa học: Comprehensive sequence analysis of horseshoe crab cuticular proteins and their involvement in transglutaminase-dependent cross-linking

Arthropod cuticles play an important role as the first barrier against inva-ding 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 designa-ted 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. . | iFEBS Journal Comprehensive sequence analysis of horseshoe crab cuticular proteins and their involvement in transglutaminase-dependent cross-linking Manabu lijima Tomonori Hashimoto Yasuyuki Matsuda Taku Nagai Yuichiro Yamano Tomohiko Ichi Tsukasa Osaki and Shun-ichiro Kawabata Department of Biology Faculty of Sciences Kyushu University Fukuoka Japan Keywords chitin-binding proteins exoskeleton horseshoe crab innate immunity transglutaminase Correspondence Shun-ichiro Kawabata Department of Biology Faculty of Sciences Kyushu University Fukuoka 812-8581 Japan Tel Fax 81 92 6422632 E-mail skawascb@ Note nucleotide sequence data are available in the DDBJ databases under the accession numbers AB201765 AB201766 AB201767 AB201768 AB201769 AB201770 AB201771 AB201772 AB201773 AB201774 AB201775 AB201776 AB201777 AB201778 and AB201779. These authors contributed equally to this work. Received 14 June 2005 revised 25 July 2005 accepted 29 July 2005 doi 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

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