Bacterial-binding activity and plasma concentration of ladderlectin in rainbow trout (Oncorhynchus mykiss)

Young, Karrie; Russell, Samantha; Smith, Marta S.; Huber, P; Ostland, V. E.; Brooks, Andrew S; Hayes, Michael; Lumsden, John S.

doi:10.1016/j.fsi.2006.10.014

Cited by 22 publications

(29 citation statements)

References 46 publications

(62 reference statements)

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Section: Discussionsupporting

confidence: 62%

“…The implications for the present experiments are not presently known. Additionally, the identity of the numerous other molecular weight bands identified on SDS-PAGE are not known; however, this is a consistent finding in previous plasma binding assays using bacteria or chitin as targets (Young et al 2007, Russell et al 2008a and demonstrates that rainbow trout have multiple PRRs that may be involved in innate defense to VHSV.That ladderlectin binds to VHSV directly suggests it may have several potential roles in defense. Direct binding of lectins to viruses can prevent infection; MBL and bovine conglutinin, independent of complement activation, inhibit the haemagglutinating ability of influenza viruses and reduce plaque formation as well as infection of neighbouring cells by interfering with attachment to cell surface targets (Kase et al 1999).…”

supporting

confidence: 60%

“…Recently VHSV has been shown to stimulate rainbow trout hepatic mRNA expression of the lectin serum amyloid A, a major acute phase reactant, via TLR signalling (Rebl et al 2009). Ladderlectin and intelectin are 2 previously identified lectins in rainbow trout (Young et al 2007, Russell et al 2008a implicated as PRRs since they bind bacterial, protozoal, and fungal pathogens. Immunohistochemical staining of healthy rainbow trout has demonstrated that both ladderlectin and intelectin are found in leukocytes and mucosal epithelia (Russell et al 2009).…”

mentioning

confidence: 99%

“…PBS-T was used as a buffer, and all incubation was conducted at room temperature with gentle agitation. A 1:5000 dilution of polyclonal rabbit anti-trout ladderlectin serum in PBS-T was used for the primary antibody, and a HRP conjugated goat anti-rabbit immunoglobulin (Dako Denmark) diluted 1:20 000 in PBS-T was used as a secondary antibody (Young et al 2007). Blots were developed with ECL-Plus Western Blotting Detection kit (GE Healthcare Biosciences) and were visualized on the Typhoon 9410 Imaging System (GE Healthcare Biosciences).…”

mentioning

confidence: 99%

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Rainbow trout Oncorhynchus mykiss ladderlectin, but not intelectin, binds viral hemorrhagic septicemia virus IVb

Reid¹,

Young²,

Lumsden³

2011

Dis. Aquat. Org.

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The innate immune system of fish is critical for rapid detection and immediate response to infection, as well as to orchestrate the adaptive branch of the immune system. Rainbow trout Oncorhynchus mykiss ladderlectin and intelectin are plasma pattern recognition receptors (PRR) for bacterial and fungal pathogens of rainbow trout, but their role as PRRs for virus is unknown. Viral hemorrhagic septicemia virus (VHSV) IVb is a recently described fish pathogen in the Great Lakes, and rainbow trout can be experimentally infected. Using an indirect enzyme-linked immunosorbent assay, rainbow trout plasma ladderlectin significantly (p < 0.05) bound purified VHSV while int electin did not. In addition, plasma ladderlectin but not intelectin was eluted from a VHSV-conjugated Toyopearl column using EDTA. Protein identification was confirmed with polyclonal antiserum used with slot immunoblot, 1-dimensional sodium dodecyl sulphate polyacrylamide electrophoresis, and Western immunoblot.KEY WORDS: Oncorhychus mykiss · Pattern recognition receptor · Viral hemorrhagic septicemia virus · Innate immunity · Plasma proteins · Binding · Ladderlectin · Intelectin Resale or republication not permitted without written consent of the publisherDis Aquat Org 95: [137][138][139][140][141][142][143] 2011 in rainbow trout by 7 d and lasting up to 21 d (Acosta et al. 2005). A DNA vaccine for VHSV conferred shortterm protection of rainbow trout Oncorhynchus mykiss from infection with heterologous rhabdoviruses and the unenveloped nodavirus of turbot (Sommerset et al. 2003). Resistance was hypothesized to be due to the initial inflammatory response that is likely to produce innate antiviral proteins such as interferon and Mx (Sommerset et al. 2003). Mx proteins are one of the major families of interferon-stimulated proteins resulting from innate immune recognition of viral infection (Ellis 2001). More recently, VHSV has been shown to stimulate multiple components of the innate immune system. In gilthead seabream Sparus aurata, VHSV has been shown to recruit and increase the activity of natural cytotoxic cells (NCC) (Esteban et al. 2008). Rainbow trout TLR9 was upregulated at the site of injection of VHSV glycoprotein G in muscle, suggesting the recruitment of dendritic cells to the site; in the head kidney and spleen there was transcriptional increase of tumor necrosis factor alpha and interleukin-6, which are cytokines known to be upregulated by TLR9 activated by unmethylated CpG DNA (Ortega-Villaizan et al. 2009). In addition, the RIG-I/MAVS pathway of double stranded RNA-stimulated interferon induction has been documented in numerous fish species (Biacchesi et al. 2009), and Mx transcript upregulation has been shown in rainbow trout (Acosta et al. 2005) in response to VHSV infection. In Japanese flounder Paralichthys olivaceus, VHSV infection upregulates the hepatic expression of C3 and complement regulatory proteins (Byon et al. 2006).Lectins are cell-associated or circulating proteins involved in recognition and binding of vir...

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Section: Discussionsupporting

confidence: 62%

supporting

confidence: 60%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Rainbow trout Oncorhynchus mykiss ladderlectin, but not intelectin, binds viral hemorrhagic septicemia virus IVb

Reid¹,

Young²,

Lumsden³

2011

Dis. Aquat. Org.

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“…salmonicida strain A449 isolated from brown trout (Michel 1979) was obtained from the National Research Council of Canada (Halifax, NS). The bacteria were cultured in tryptic soy broth at 16°C for 48-72 h. Recombinant lectin binding to A. salmonicida experiments were performed as described (Brooks et al 2003;Lillie et al 2006;Young et al 2007), with minor changes. Briefly, 5 mL cultures of A. salmonicida were grown to an OD 600nm of approximately 0.8.…”

Section: Bacterial Binding Assaymentioning

confidence: 99%

Expression of recombinant Atlantic salmon serum C-type lectin in Drosophila melanogaster Schneider 2 cells

et al. 2012

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The Atlantic salmon (Salmo salar) serum lectin (SSL) is a soluble C-type lectin that binds bacteria, including salmon pathogens. This lectin is a cysteine-rich oligomeric protein. Consequently, a Drosophila melanogaster expression system was evaluated for use in expressing SSL. A cDNA encoding SSL was cloned into a vector designed to express it as a fusion protein with a hexahistidine tag, under the control of the Drosophila methallothionein promoter. The resulting construct was stably transfected into Drosophila S2 cells. After CdCl 2 induction, transfected S2 cells secreted recombinant SSL into the cell culture medium. A cell line derived from stably transformed polyclonal cell populations expressing SSL was used for large-scale expression of SSL. Recombinant SSL was purified from the culture medium using a two-step purification scheme involving affinity binding to yeast cells and metal-affinity chromatography. Although yields of SSL were very low, correct folding and functionality of the recombinant SSL purified in this manner was demonstrated by its ability to bind to Aeromonas salmonicida. Therefore, Drosophila S2 cells may be an ideal system for the production of SSL if yields can be increased.

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Expressed Sequences and Polymorphisms in Rohu Carp (Labeo rohita, Hamilton) Revealed by mRNA-seq

et al. 2012

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Expressed genes and polymorphisms were identified in lines of rohu Labeo rohita selected for resistance or susceptibility to Aeromonas hydrophila, an important bacterial pathogen causing aeromoniasis. All animals were grown in a common environment and RNA from ten individuals from each line pooled for Illumina mRNA-seq. De novo transcriptome assembly produced 137,629 contigs with 40× average coverage.Forty-four percent of the assembled sequences were annotated with gene names and ontology terms. Of these, 3,419 were assigned biological process terms related to "stress response" and 1,939 "immune system". Twenty-six contigs containing 38 single nucleotide polymorphisms (SNPs) were found to map to the Cyprinus carpio mitochondrial genome and over 26,000 putative SNPs and 1,700 microsatellite loci were detected. Seventeen percent of the 100 transcripts with coverage data most indicative of higher-fold expression(>5.6 fold) in the resistant line pool showed homology to major histocompatibility (MH), heat shock proteins (HSP)30, 70 and 90, glycoproteins or serum lectin genes with putative functions affecting immune response. Forty-one percent of these 100 transcripts showed no or low homology to known genes. Of the SNPs identified, 96 showing the highest allele frequency differences between susceptible and resistant line fish included transcripts with homology to MH class I and galactoside-binding soluble lectin, also with putative functions affecting innate and acquired immune response. A comprehensive sequence resource for L. rohita, including annotated microsatellites and SNPs from a mixture of A. hydrophila-susceptible and -resistant individuals, was created for subsequent experiments aiming to identify genes associated with A. hydrophila resistance.

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Bacterial-binding activity and plasma concentration of ladderlectin in rainbow trout (Oncorhynchus mykiss)

Cited by 22 publications

References 46 publications

Rainbow trout Oncorhynchus mykiss ladderlectin, but not intelectin, binds viral hemorrhagic septicemia virus IVb

Rainbow trout Oncorhynchus mykiss ladderlectin, but not intelectin, binds viral hemorrhagic septicemia virus IVb

Expression of recombinant Atlantic salmon serum C-type lectin in Drosophila melanogaster Schneider 2 cells

Expressed Sequences and Polymorphisms in Rohu Carp (Labeo rohita, Hamilton) Revealed by mRNA-seq

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