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1.
J Virol ; 83(1): 347-56, 2009 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-18945787

RESUMEN

C-type lectins play key roles in pathogen recognition, innate immunity, and cell-cell interactions. Here, we report a new C-type lectin (C-type lectin 1) from the shrimp Litopenaeus vannamei (LvCTL1), which has activity against the white spot syndrome virus (WSSV). LvCTL1 is a 156-residue polypeptide containing a C-type carbohydrate recognition domain with an EPN (Glu(99)-Pro(100)-Asn(101)) motif that has a predicted ligand binding specificity for mannose. Reverse transcription-PCR analysis revealed that LvCTL1 mRNA was specifically expressed in the hepatopancreas of L. vannamei. Recombinant LvCTL1 (rLvCTL1) had hemagglutinating activity and ligand binding specificity for mannose and glucose. rLvCTL1 also had a strong affinity for WSSV and interacted with several envelope proteins of WSSV. Furthermore, we showed that the binding of rLvCTL1 to WSSV could protect shrimps from viral infection and prolong the survival of shrimps against WSSV infection. Our results suggest that LvCTL1 is a mannose-binding C-type lectin that binds to envelope proteins of WSSV to exert its antiviral activity. To our knowledge, this is the first report of a shrimp C-type lectin that has direct anti-WSSV activity.


Asunto(s)
Enfermedades de los Animales/prevención & control , Antivirales/farmacología , Lectinas Tipo C/metabolismo , Penaeidae/virología , Virus del Síndrome de la Mancha Blanca 1/efectos de los fármacos , Secuencias de Aminoácidos , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Sitios de Unión , Perfilación de la Expresión Génica , Glucosa/metabolismo , Hepatopáncreas/metabolismo , Manosa/metabolismo , Datos de Secuencia Molecular , Unión Proteica , Estructura Terciaria de Proteína , Alineación de Secuencia , Análisis de Supervivencia
2.
Fish Shellfish Immunol ; 26(3): 473-82, 2009 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-19340946

RESUMEN

The NF-kappaB/IkappaBalpha pathway plays an important role in the regulation of immune and inflammatory responses. IkappaBalpha is an inhibitory molecule that sequesters transcription activator NF-kappaB dimer in the cytoplasm of unstimulated cells. Here, we isolated the full-length cDNAs of the mandarin fish (Siniperca chuatsi) alpha inhibitor of NF-kappaB (ScIkappaBalpha) and p65 NF-kappaB (Scp65). Multiple sequence alignments showed that the amino acid sequences of both ScIkappaBalpha and Scp65 contain conserved domains similar to those of mammalian counterparts. Protein pull-down and coimmunoprecipitation assays showed that ScIkappaBalpha directly bound with Scp65. Real-time quantitative PCR analysis showed that ScIkappaBalpha mRNA was constitutive in all mandarin fish tissues detected. After challenge with infectious spleen and kidney necrosis virus (ISKNV), the mRNA level of ScIkappaBalpha was decreased nearly 6 fold in the spleen. This result suggests that the NF-kappaB/IkappaBalpha pathway in mandarin fish may play a role in the immune response against ISKNV.


Asunto(s)
Enfermedades de los Peces/metabolismo , Proteínas I-kappa B/metabolismo , Perciformes/genética , Perciformes/metabolismo , Factor de Transcripción ReIA/metabolismo , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Infecciones por Virus ADN/metabolismo , Perfilación de la Expresión Génica , Regulación de la Expresión Génica , Proteínas I-kappa B/química , Iridoviridae/fisiología , Modelos Moleculares , Datos de Secuencia Molecular , Inhibidor NF-kappaB alfa , Unión Proteica , Estructura Terciaria de Proteína , Alineación de Secuencia , Factor de Transcripción ReIA/química
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