A novel C-type lectin from Eriocheir sinensis functions as a pattern recognition receptor with antibacterial activity

Journal Article A Chimeric Lectin Formed from Bauhinia purpurea Lectin and Lens culinaris Lectin Recognizes a Unique Carbohydrate Structure Get access Kazuo Yamamoto, Kazuo Yamamoto 2 Laboratory of Molecular Medicine, Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo7–3–1 Hongo, Bunkyo-ku, Tokyo 113–0033 2 To whom correspondence should be addressed. Tel +81-3-5841-4776, 8843, Fax: +81-03-5841-8923, E-mail:yamamoto@k.u-tokyo.ac.jp Search for other works by this author on: Oxford Academic PubMed Google Scholar Yukiko Konami, Yukiko Konami Laboratory of Molecular Medicine, Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo7–3–1 Hongo, Bunkyo-ku, Tokyo 113–0033 Search for other works by this author on: Oxford Academic PubMed Google Scholar Toshiaki Osawa Toshiaki Osawa Laboratory of Molecular Medicine, Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo7–3–1 Hongo, Bunkyo-ku, Tokyo 113–0033 Search for other works by this author on: Oxford Academic PubMed Google Scholar The Journal of Biochemistry, Volume 127, Issue 1, January 2000, Pages 129–135, https://doi.org/10.1093/oxfordjournals.jbchem.a022573 Published: 01 January 2000 Article history Received: 02 September 1999 Accepted: 25 October 1999 Published: 01 January 2000

C-type lectin

CD69

10.1093/oxfordjournals.jbchem.a022573

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Citations (27)

Purification, characterization, and cDNA cloning of -N-acetylgalactosamine-specific lectin from starfish, Asterina pectinifera

Glycobiology (2002)

Masato Kakiuchi Nozomu Okino Noriyuki Sueyoshi Sachiyo Ichinose A Omori

We report here the purification, characterization, and cDNA cloning of a novel N-acetylgalactosamine-specific lectin from starfish, Asterina pectinifera. The purified lectin showed 19-kDa, 41-kDa, and 60-kDa protein bands on SDS–PAGE, possibly corresponding to a monomer, homodimer, and homotrimer. Interestingly, on 4–20% native PAGE the lectin showed at least nine protein bands, among which oligomers containing six to nine subunits had potent hemagglutination activity for sheep erythrocytes. The hemagglutination activity of the lectin was specifically inhibited by N-acetylgalactosamine, Tn antigen, and blood group A trisaccharide, but not by N-acetylglucosamine, galactose, galactosamine, or blood group B trisaccharide. The specificity of the lectin was further examined using various glycosphingolipids and biotin-labeled lectin. The lectin was found to bind to Gb5Cer, but not Gb4Cer, Gb3Cer, GM1a, GM2, or asialo-GM2, indicating that the lectin specifically binds to the terminal α-GalNAc at the nonreducing end. The hemagglutination activity of the lectin was completely abolished by chelation with EDTA or EGTA and completely restored by the addition of CaCl2. cDNA cloning of the lectin showed that the protein is composed of 168 amino acids, including a signal sequence of 18 residues, and possesses the typical C-type lectin motif. These findings indicate that the protein is a C-type lectin. The recombinant lectin, produced in a soluble form by Escherichia coli, showed binding activity for asialomucin in the presence of Ca2+ but no hemagglutination.

Cloning (programming)

C-type lectin

10.1093/glycob/12.2.85

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Citations (27)

F-type Lectin Domains: Provenance, Prevalence, Properties, Peculiarities, and Potential

Advances in experimental medicine and biology (2018)

Sonal Mahajan T.N.C. Ramya

C-type lectin

Galectin

10.1007/978-981-13-3065-0_24

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Citations (2)

Characterisation of a mannose-binding C-type lectin from Oxyuranus scutellatus snake venom

Biochimie (2010)

Stephen Earl Jonathan P. Robson Manuela Trabi John de Jersey Paul P. Masci

C-type lectin

10.1016/j.biochi.2010.11.006

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Citations (16)

Molecular cloning, characterization and expression analysis of F-type lectin from pearl oyster Pinctada fucata

Fish & Shellfish Immunology (2013)

A. Anju Joseph Jeswin P C Thomas K.K. Vijayan

Pinctada fucata

C-type lectin

Ficolin

Cloning (programming)

10.1016/j.fsi.2013.03.359

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Citations (23)

Crystal structure of an L‐type lectin domain from archaea

Proteins Structure Function and Bioinformatics (2022)

Farha Khan K. Suguna

Abstract The crystal structures of an L‐type lectin domain from Methanocaldococcus jannaschii in apo and mannose‐bound forms have been determined. A thorough investigation of L‐type lectin domains from several organisms provides insight into the differences in these domains from different kingdoms of life. While the overall fold of the L‐type lectin domain is conserved, differences in the lengths of the carbohydrate‐binding loops and significant variations in the Mn 2+ ‐binding site compared to the Ca 2+ ‐binding site are observed. Furthermore, the sequence and phylogenetic analyses suggest that the archaeal L‐type lectin domain is evolutionarily closer to the plant legume lectins than to its bacterial or animal counterparts. This is the first report of the biochemical, structural, sequence, and phylogenetic analyses of an L‐type lectin domain from archaea and serves to enhance our understanding of the species‐specific differences and evolution of L‐type lectin domains.

C-type lectin

10.1002/prot.26440

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Citations (2)

Oligomerisation and carbohydrate binding in an Atlantic salmon serum C-type lectin consistent with non-self recognition

Fish & Shellfish Immunology (2004)

Lewis P. Stratton

C-type lectin

10.1016/j.fsi.2004.04.006

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Citations (15)

A novel C-type lectin from Eriocheir sinensis functions as a pattern recognition receptor with antibacterial activity