A novel C-type lectin with two CRD domains from Chinese shrimp Fenneropenaeus chinensis functions as a pattern recognition protein

Zhang, Xiaowen; Xu, Wenteng; Wang, Xianwei; Mu, Yi; Zhao, Xiao‐Fan; Yu, Xiao‐Qiang; Wang, Jinxing

doi:10.1016/j.molimm.2009.02.029

Cited by 153 publications

(68 citation statements)

References 54 publications

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“…Crustaceans' hepatopancreas is crucial for the immune system as it is the main production site for immune recognition molecules. Similar to most reported shrimp C-type lectins [19,25,26], Chinese mitten crab EsCTLDcp-1 and EsCTLDcp-2 transcripts were mainly detected in hepatopancreas of normal crabs. In Chinese shrimp, the transcripts of C-type lectin genes were increased at 2 h in hepatopancreas from shrimps challenged with bacteria, but returned to normal level quickly [26,45].…”

Section: Discussionsupporting

confidence: 83%

“…Similar to most reported shrimp C-type lectins [19,25,26], Chinese mitten crab EsCTLDcp-1 and EsCTLDcp-2 transcripts were mainly detected in hepatopancreas of normal crabs. In Chinese shrimp, the transcripts of C-type lectin genes were increased at 2 h in hepatopancreas from shrimps challenged with bacteria, but returned to normal level quickly [26,45]. However the expression of shrimp C-type lectin gene containing one CTLD domain such as FcLec3 in hepatopancreas from shrimps challenged with bacteria was increased from 2 h until 24 h [21].…”

Section: Discussionsupporting

confidence: 83%

“…Shrimp CTLs have been reported to be involved in various biological processes including anti-virus response [23], anti-bacteria response [24], anti-microbial activity [25] or functioning as a pattern recognition protein [26]. However, only a few are known to the innate immune system of Chinese mitten crab, and no literature on Chinese mitten crab CTLs.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of two C-type lectin-like domain (CTLD)-containing proteins from the cDNA library of Chinese mitten crab Eriocheir sinensis

Guo

Zou

et al. 2011

Fish & Shellfish Immunology

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Section: Discussionsupporting

confidence: 83%

Section: Discussionsupporting

confidence: 83%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of two C-type lectin-like domain (CTLD)-containing proteins from the cDNA library of Chinese mitten crab Eriocheir sinensis

Guo

Zou

et al. 2011

Fish & Shellfish Immunology

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“…Estas lectinas han sido descritas en varias especies de crustáceos Fenneropenaeus chinensis (Sun et al, 2008;Zhan et al, 2009;Xu et al, 2010) en Litopenaeus vannamei (Zhan et al, 2009a(Zhan et al, , 2009b. Song et al (2014) sugiere una interacción directa entre los MOS y el sistema inmune innato de crustáceos a través de algunos PRRs con afinidad por manosa (Sun et al, 2008;Arockiaraj et al, 2015), los cuales a su vez presentan alta especifidad de reconocimiento de PAMPs asociados a V. angillarum, E. coli y WSSV (Sun et al, 2008;Zhang et al, 2009aZhang et al, , 2009bZhao et al, 2009;Xu et al, 2010). Se ha sugerido que estos PRRs están generalmente vinculados a la vía del complemento (Arockiaraj et al, 2015;Clark & Greenwood, 2016), pero existen carencias investigativas sobre este aspecto en particular (Clark & Greenwood, 2016).…”

Section: Vías Documentadasunclassified

Manano oligosacaridos como prebioticos en acuicultura de crustaceos

Gainza¹,

Romero²

2017

lajar

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RESUMEN.Los prebióticos tienen el potencial de incrementar la eficiencia y sostenibilidad de la producción acuícola. Uno de los prebióticos más promisorios en acuicultura son los Manano oligosacáridos (MOS). Estos MOS son moléculas de carbohidratos complejos derivados de la pared de la célula de la levadura Saccharomyces cerevisiae, que impiden la adhesión de patógenos bacterianos porque actúan bloqueando la adherencia de las lectinas microbianas con los carbohidratos presentes en la superficie de las células intestinales. Esta prevención de la adhesión impide la colonización y proceso infectivo de los patógenos. La ventaja del uso de MOS es que puede prevenir infecciones a través de mecanismos diferentes a los utilizados por los antibióticos. Este artículo muestra los avances obtenidos en uso de MOS como prebióticos en la acuicultura, en particular en el cultivo de crustáceos, donde han generado respuestas positivas en todas las experiencias actuando sobre el incremento del crecimiento, la supervivencia, modulando la respuesta inmune y modificando la morfología del tracto digestivo. La identificación de las cepas que son promovidas o excluidas y la caracterización de la acción moduladora en la microbiota resultante quedan abiertas como uno de los campos a desarrollar en conjunto con la extensión de estos resultados a la práctica productiva. Palabras clave: crustáceos, manano oligosacáridos, MOS, prebióticos, microbiota, crecimiento. Mannan oligosaccharides as prebiotics in crustacean aquacultureABSTRACT. Probiotics have the potential to increase the efficiency and sustainability of aquaculture production. The mannan-oligosaccharides (MOS) are complex carbohydrates derived from the cell wall of the yeast Saccharomyces cerevisiae, which act by blocking adherence of bacterial lectins to carbohydrates on the surface of intestinal cells; this action prevents colonization and infection processes carried out by bacterial pathogens. In this work, we review the current evidence about the use of MOS as prebiotics in shellfish aquaculture, enlightening the positive responses in most of the experiences, such as improvement in growth and survival, modulating the immune response and modifying the morphology of the digestive tract. The identification of strains that are promoted or excluded, and the characterization of the resulting modulating action in gut´s microbiota, remains open as one of the fields to be developed in conjunction with the extension of these results to the productive practice.

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“…The cloned and purified penaeid shrimp C-type lectins fall into two structurally related classes of proteins: those containing a single CTLD with a spacer region between the signal peptide (Ma et al, 2007;Sun et al, 2008a;Zhang et al, 2009b), and those with two CRDs disposed in tandem with spacer regions between the signal peptide and the CRD1 that intervenes between CRD1 and CRD2 (Ma et al, 2008;Zhang et al, 2009b). These shrimp C-type lectins were shown to recognize and bind with high affinity to galactose, mannose, N-acetyl glucosamine, N-acetyl galactosamine, and N-acetyl mannosamine, as well as to disaccharides, such as maltose and trehalose, to some degree (Rittidach et al, 2007;Ma et al, 2008;Zhang et al, 2009c).…”

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.

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A novel C-type lectin with two CRD domains from Chinese shrimp Fenneropenaeus chinensis functions as a pattern recognition protein

Cited by 153 publications

References 54 publications

Characterization of two C-type lectin-like domain (CTLD)-containing proteins from the cDNA library of Chinese mitten crab Eriocheir sinensis

Characterization of two C-type lectin-like domain (CTLD)-containing proteins from the cDNA library of Chinese mitten crab Eriocheir sinensis

Manano oligosacaridos como prebioticos en acuicultura de crustaceos

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

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