Development of an in situ hybridisation procedure for the detection of sole aquabirnavirus in infected fish cell cultures

Alonso, M. Carmen; Cano, Irene; Castro, Dolores; Pérez-Prieto, Sara I.; Borrego, Juan J.

doi:10.1016/j.jviromet.2003.11.003

Cited by 23 publications

(12 citation statements)

References 16 publications

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“…During virus maturation, pVP2 is cleaved to become VP2, the major outer capsid protein with neutralization epitopes [28,47]. A 613-bp VP2 cDNA probe has turned out to be a useful tool to detect solevirus in infected fish cells [48]. Moreover, IPNV VP2 transcript levels were successfully used to study viral replication in Atlantic salmon parr [45,49].…”

Section: Discussionmentioning

confidence: 99%

Poly I:C induces Mx transcription and promotes an antiviral state against sole aquabirnavirus in the flatfish Senegalese sole (Solea senegalensis Kaup)

Fernández-Trujillo

Ferro

García-Rosado

et al. 2008

Fish & Shellfish Immunology

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Section: Discussionmentioning

confidence: 99%

Poly I:C induces Mx transcription and promotes an antiviral state against sole aquabirnavirus in the flatfish Senegalese sole (Solea senegalensis Kaup)

Fernández-Trujillo

Ferro

García-Rosado

et al. 2008

Fish & Shellfish Immunology

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“…In situ hybridization was performed on tissue sections (7 mm) according to Alonso et al [29]. Antisense (AS) and sense (S) probes were synthesized based on the DlFBL cDNA clone.…”

Section: In Situ Hybridizationmentioning

confidence: 99%

F-type lectin from the sea bass (Dicentrarchus labrax): Purification, cDNA cloning, tissue expression and localization, and opsonic activity

Salerno

Parisi

Parrinello

et al. 2009

Fish & Shellfish Immunology

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Recently described biochemical and structural aspects of fucose-binding lectins from the European eel (Anguilla anguilla) and striped bass (Morone saxatilis) led to the identification of a novel lectin family ("F-type" lectins) characterized by a unique sequence motif and a characteristic structural fold. The F-type fold is shared not only with other members of this lectin family, but also with apparently unrelated proteins ranging from prokaryotes to vertebrates. Here we describe the purification, biochemical and molecular properties, and the opsonic activity of an F-type lectin (DlFBL) isolated from sea bass (Dicentrarchus labrax) serum. DlFBL exhibits two tandemly arranged carbohydrate-recognition domains that display the F-type sequence motif. In situ hybridization and immunohistochemical analysis revealed that DlFBL is specifically expressed and localized in hepatocytes and intestinal cells. Exposure of formalin-killed Escherichia coli to DlFBL enhanced their phagocytosis by D. labrax peritoneal macrophages relative to the unexposed controls, suggesting that DlFBL may function as an opsonin in plasma and intestinal mucus.

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“…After plasmid amplification, DNA was purified by using a QUIAquick Gel Extraction Kit and specific primers. Tissue sections (5 µm) were prepared on coated glass slides and in situ hybridization was performed according to Alonso et al (2004). Sections were deparaffinized, washed twice in PBS-T and digested with proteinase K (1 μl/ml in PBS-T).…”

Section: Immunohistochemistrymentioning

confidence: 99%

A serum fucose-binding lectin (DlFBL) from adult Dicentrarchus labrax is expressed in larva and juvenile tissues and contained in eggs

et al. 2010

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The purification, cloning, sequencing, molecular properties and expression of a fucose-binding lectin from the serum of Dicentrarchus labrax (DlFBL) have been previously reported. We now describe the distribution and expression of DlFBL during fish ontogeny. Immunohistochemistry and in situ hybridization assays were carried out at various developmental stages (from 10 days post-hatching larvae to juveniles). Another fucose-binding lectin, similar to DlFBL in biochemical, immunochemical and agglutinating properties, was extracted and purified from eggs and appeared to be localized in the embryo yolk sack residual. DlFBL was found in columnar and goblet cells of the intestinal epithelium of larvae (from 20 days post-hatching) and juveniles and in parenchymal tissue of juveniles. DlFBL mRNA and protein were detected in the intestinal epithelium and in hepatocytes. An amplification product from degenerate primers indicates that lectin isotypes with DlFBL epitopes are expressed in eggs and embryos. Whether the lectin fraction isolated from eggs and embryos includes DlFBL of maternal origin remains unclear.

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Development of an in situ hybridisation procedure for the detection of sole aquabirnavirus in infected fish cell cultures

Cited by 23 publications

References 16 publications

Poly I:C induces Mx transcription and promotes an antiviral state against sole aquabirnavirus in the flatfish Senegalese sole (Solea senegalensis Kaup)

Poly I:C induces Mx transcription and promotes an antiviral state against sole aquabirnavirus in the flatfish Senegalese sole (Solea senegalensis Kaup)

F-type lectin from the sea bass (Dicentrarchus labrax): Purification, cDNA cloning, tissue expression and localization, and opsonic activity

A serum fucose-binding lectin (DlFBL) from adult Dicentrarchus labrax is expressed in larva and juvenile tissues and contained in eggs

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