Identification and comparative analysis of three novel C-type lectins from the silkworm with functional implications in pathogen recognition

Takase, Hinako M.; Watanabe, Ayako; Yoshizawa, Yasutaka; Kitami, Madoka; Satō, Ryōichi

doi:10.1016/j.dci.2009.01.005

Cited by 47 publications

(35 citation statements)

References 36 publications

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“…Oculina tachylectin-2, which has a structure similar to crab tachylectin-2, has high amino acid diversity, and positive selection has been observed in it [43]. Taken together, positive selection in shrimp dual-CRD-containing lectins suggests their roles in shrimp innate immunity and positive selection-induced amino acid diversity of lectins may confer their ability to recognize a broad range of microbes (Table 3).…”

Section: Evolutionary Analysis Of Shrimp and Prawns C-type Lectin Genmentioning

confidence: 93%

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Immune response of four dual-CRD C-type lectins to microbial challenges in giant freshwater prawn Macrobrachium rosenbergii

Ren

et al. 2012

Fish & Shellfish Immunology

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Section: Evolutionary Analysis Of Shrimp and Prawns C-type Lectin Genmentioning

confidence: 93%

“…The N-terminal CRD was shorter in length, whereas the C-terminal was longer. The short form had four cysteines while the long form had six [43]. The different lengths of CRDs of M. rosenbergii mainly result from the different numbers of residues between the third and fourth cysteines.…”

Section: Tissue Distribution and Expression Pattern Analysis Of Mrlecmentioning

confidence: 98%

Immune response of four dual-CRD C-type lectins to microbial challenges in giant freshwater prawn Macrobrachium rosenbergii

Ren

et al. 2012

Fish & Shellfish Immunology

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“…By now, more than 30 encoded C-type lectin-like domains have been identified in the fruit fly Drosophila melanogaster (15). The first C-type lectin from the silkworm Bombyx mori called LPS-binding protein (BmLBP) was isolated and characterized in 1997 (16) and then its cDNA cloning was described in 1999 (17). And in Manduca sexta , four immulectins (IML1-4) have been reported to stimulate prophenoloxidase activation and promote hemocyte encapsulation as important PRRs (18-21).…”

Section: Introductionmentioning

confidence: 99%

A novel pattern recognition protein of the Chinese oak silkmoth, Antheraea pernyi, is involved in the pro-PO activating system

Wang

Zhang²,

Chen³

et al. 2013

BMB Reports

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In this paper, we firstly reported a C-type lectin cDNA clone of 1029 bps from the larvae of A. Pernyi (Ap-CTL) using PCR and RACE techniques. The full-length cDNA contains an open reading frame encoding 308 amino acid residues which has two different carbohydrate-recognition domains (CRDs) arranged in tandem. To investigate the biological activities in the innate immunity, recombinant Ap-CTL was expressed in E. coli with a 6-histidine at the amino-terminus (Ap-rCTL). Besides acted as a broad-spectrum recognition protein binding to a wide range of PAMPs and microorganisms, Ap-rCTL also had the ability to recognize and trigger the agglutination of bacteria and fungi. In the proPO activation assay, Ap-rCTL specifically restored the PO activity of hemolymph blocked by anti-Ap-rCTL antibody in the presence of different PAMPs or microorganisms. In summary, Ap-rCTL plays an important role in insect innate immunity as an pattern recognition protein. [BMB Reports 2013; 46(7): 358-363]

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“…In silkworms, three homologs were found to be expressed in the testis and ovary that act as primary PRRs in Bombyx mori cellular immunity (Takase et al, 2009). Additionally, C-type lectins with two CRDs arranged in tandem function as pattern recognition receptors in the cotton bollworm, promoting hemocyte phagocytosis of pathogens, protecting the insect from bacterial infection (Tian et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Cloning and molecular modeling of Litopenaeus vannamei (Penaeidae) C-type lectin homologs with mutated mannose binding domain-2

Costa

Valença²,

Silva³

et al. 2011

Genet. Mol. Res.

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ABSTRACT. C-type lectins are animal proteins that contain at least one carbohydrate recognition domain (CRD) capable of mediating sugar and calcium binding. Carbohydrate recognition is directly required for some biological functions, including the innate immune response. We cloned two novel C-type lectin (CTL) precursors from the commercial marine shrimp Litopenaeus vannamei. The cloned cDNAs encompass ORFs of 1044 nucleotides and encode highly similar two- Cloning and molecular modeling of Litopenaeus vannamei domain polypeptides of 347 residues. The predicted proteins, LvCTLbr1 and -br2, contain the consensus triad that recognizes galactose (-GlnProAsp-) in CRD1 but also contain a mutated mannose-binding site (-GluProAsn-) in the second domain (CRD2). Phylogenetic analysis of LvCTL-br1 and -br2 and hundreds of CTL-like domaincontaining proteins have allowed grouping of penaeid shrimp CTLs into three functional clusters. Reverse transcription coupled to PCR indicated that LvCTL-br1 expression is induced in shrimp gills upon IHHNV infection. Computational molecular modeling of LvCTL-br1 and -br2 revealed that three amino acid substitutions in CRD1 occur near the sugar binding site. Also, the 3-D models show a long loop of LvCTL-br1 CRD2 that might accommodate complex sugars. The structural data, evolutionary history and functional analysis support the hypothesis that gene duplication and accelerated evolution have caused functional diversification of penaeid shrimp C-type lectins.

show abstract

Identification and comparative analysis of three novel C-type lectins from the silkworm with functional implications in pathogen recognition

Cited by 47 publications

References 36 publications

Immune response of four dual-CRD C-type lectins to microbial challenges in giant freshwater prawn Macrobrachium rosenbergii

Immune response of four dual-CRD C-type lectins to microbial challenges in giant freshwater prawn Macrobrachium rosenbergii

A novel pattern recognition protein of the Chinese oak silkmoth, Antheraea pernyi, is involved in the pro-PO activating system

Cloning and molecular modeling of Litopenaeus vannamei (Penaeidae) C-type lectin homologs with mutated mannose binding domain-2

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