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1.
Fish Shellfish Immunol ; 63: 189-195, 2017 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-28214599

RESUMEN

Toll-like receptors (TLRs) play an important role in the activation of innate immune response but their functions in bivalves remain largely unknown. In this study, we identified a TLR from the freshwater pearl mussel Hyriopsis cumingii (HcToll3) and investigated its functions in immunity. The full-length cDNA of HcToll3 is 3852 bp and includes an open reading frame (ORF) of 3228 bp that encodes a polypeptide of 1075 amino acids. The predicted HcToll3 protein shares similar structural characteristics with other known Toll family proteins. Quantitative real-time PCR analysis revealed that HcToll3 mRNA is broadly expressed in all of the examined tissues; its transcript level was significantly up-regulated by challenge with gram-negative bacteria Vibrio parahaemolyticus or lipopolysaccharide, but not gram-positive Staphylococcus aureus or peptidoglycan. RNA interference by siRNA results showed that HcToll3 regulated expression of whey acidic protein (HcWAP) and lysozymes (HcLyso1 and HcLyso2) in vivo and knockdown of HcToll3 suppressed the elimination of V. parahaemolyticus. These findings suggest that HcToll3 might be involved in anti-Vibrio defense in H. cumingii.


Asunto(s)
Inmunidad Innata , Receptor Toll-Like 3/genética , Unionidae/genética , Unionidae/inmunología , Vibrio parahaemolyticus/fisiología , Animales , Reacción en Cadena en Tiempo Real de la Polimerasa , Análisis de Secuencia de ADN , Receptor Toll-Like 3/metabolismo , Unionidae/microbiología
2.
Zool Res ; 45(1): 25-35, 2024 Jan 18.
Artículo en Inglés | MEDLINE | ID: mdl-38114430

RESUMEN

Long non-coding RNAs (lncRNAs) function as key modulators in mammalian immunity, particularly due to their involvement in lncRNA-mediated competitive endogenous RNA (ceRNA) crosstalk. Despite their recognized significance in mammals, research on lncRNAs in lower vertebrates remains limited. In the present study, we characterized the first immune-related lncRNA (pol-lnc78) in the teleost Japanese flounder ( Paralichthys olivaceus). Results indicated that pol-lnc78 acted as a ceRNA for pol-miR-n199-3p to target the sterile alpha and armadillo motif-containing protein (SARM), the fifth discovered member of the Toll/interleukin 1 (IL-1) receptor (TIR) adaptor family. This ceRNA network regulated the antibacterial responses of flounder via the Toll-like receptor (TLR) signaling pathway. Specifically, SARM acted as a negative regulator and exacerbated bacterial infection by inhibiting the expression of inflammatory cytokines IL-1ß and tumor necrosis factor-α (TNF-α). Pol-miR-n199-3p reduced SARM expression by specifically interacting with the 3' untranslated region (UTR), thereby promoting SARM-dependent inflammatory cytokine expression and protecting the host against bacterial dissemination. Furthermore, pol-lnc78 sponged pol-miR-n199-3p to ameliorate the inhibition of SARM expression. During infection, the negative regulators pol-lnc78 and SARM were significantly down-regulated, while pol-miR-n199-3p was significantly up-regulated, thus favoring host antibacterial defense. These findings provide novel insights into the mechanisms underlying fish immunity and open new horizons to better understand ceRNA crosstalk in lower vertebrates.


Asunto(s)
Lenguado , MicroARNs , ARN Largo no Codificante , Animales , Citocinas/metabolismo , Regulación hacia Abajo , Lenguado/genética , Lenguado/metabolismo , MicroARNs/genética , MicroARNs/metabolismo , ARN Endógeno Competitivo , ARN Largo no Codificante/genética
3.
Fish Shellfish Immunol ; 34(5): 1287-93, 2013 May.
Artículo en Inglés | MEDLINE | ID: mdl-23454418

RESUMEN

Toll receptor was first discovered in Drosophila and has an important function in the innate immunity of invertebrates. In this study, the Toll receptor HcToll1 from Hyriopsis cumingii with a full length of 3810 bp consisting of a 3687 bp ORF that encodes a total of 1228 amino acids protein was selected for further study. The HcToll1 protein consisted of a signal peptide, 17 LRR domains, 2 LRRCT domains, 1 LRRNT domain, 1 TM domain, and 1 TIR domain. Phylogenetic analysis results showed that HcToll1 was clustered in one group together with other mollusca tolls. RT-PCR analysis results showed that HcToll1 was expressed in all tested tissues such as hemocytes, hepatopancreas, gills, and mantle. qRT-PCR analysis results showed that HcToll1 expression was increased by the presence of Escherichia coli, Vibrio anguillarum, Staphyloccocus aureus, and White Spot Syndrome Virus (WSSV). Over-expression of HcTIR could up-regulate expression of drosomycin gene in Drosophila S2 cells. The results of our study indicated that HcToll1 is a functional Toll and it has an important function in the generation of innate immune responses of H. cumingii against microbial challenge.


Asunto(s)
Receptor Toll-Like 1/genética , Receptor Toll-Like 1/inmunología , Unionidae/genética , Unionidae/inmunología , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Clonación Molecular , ADN Complementario/genética , ADN Complementario/metabolismo , Escherichia coli/fisiología , Regulación de la Expresión Génica , Datos de Secuencia Molecular , Especificidad de Órganos , Filogenia , ARN/genética , ARN/metabolismo , Reacción en Cadena en Tiempo Real de la Polimerasa , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Alineación de Secuencia , Staphylococcus aureus/fisiología , Receptor Toll-Like 1/química , Unionidae/química , Vibrio/fisiología , Virus del Síndrome de la Mancha Blanca 1/fisiología
4.
Gen Comp Endocrinol ; 162(2): 192-202, 2009 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-19327361

RESUMEN

Three cDNA sequences encoding the gonadotropin subunits, common glycoprotein alpha subunit (GTHalpha), FSHbeta and LHbeta subunits were isolated from marbled eel. The cDNA of GTHalpha encodes 116 amino acids with a signal peptide of 24 amino acids and a mature peptide of 92 amino acids. The FSHbeta subunit consists of 127 amino acids with a 22 amino acid signal peptide and a 105 amino acid mature peptide, while the LHbeta subunit consists of 140 amino acids with a 24 amino acid signal peptide and a 116 amino acid mature peptide. Comparison of the deduced amino acid sequences of marbled eel GTHalpha, FSHbeta, and LHbeta with that of other fishes shows a high degree of conservation in the number of cysteine residues and potential N-linked glycosylation sites. The mRNA of GTHalpha, FSHbeta and LHbeta were not only detected in pituitary, but also in ovary and testes by RT-PCR. Quantitative realtime PCR analysis revealed that the GTHalpha and LHbeta transcriptional levels in pituitaries of female and male eels gradually increased during the artificially inducing gonadal development, and peaked at late vitellogenic stage and spermiation stage, respectively. FSHbeta mRNA in the pituitaries of female eels maintained a high level at previtellogenic stage, early vitellogenic stage as well as mid-vitellogenic stage but declined sharply at late vitellogenic stage and migratory nucleus stage. In male eels, the mRNA levels of FSHbeta in the pituitaries were higher at early spermatogenesis stage than at both late spermatogenesis stage and spermiation stage. These results suggested that FSH would be in control of initiation and maintenance of gonadal growth and gametogenesis, whereas LH would be involved in the final gonadal maturation and spermiation/ovulation in the tropic eel Anguilla marmorata.


Asunto(s)
Anguilla/metabolismo , Gonadotropinas/genética , Subunidades de Proteína/genética , Secuencia de Aminoácidos , Anguilla/genética , Anguilla/crecimiento & desarrollo , Animales , Secuencia de Bases , Clonación Molecular , Femenino , Gonadotropinas/química , Gonadotropinas/metabolismo , Masculino , Datos de Secuencia Molecular , Ovario/efectos de los fármacos , Ovario/crecimiento & desarrollo , Ovario/metabolismo , Filogenia , Subunidades de Proteína/química , Subunidades de Proteína/metabolismo , ARN Mensajero/metabolismo , Alineación de Secuencia , Testículo/efectos de los fármacos , Testículo/crecimiento & desarrollo , Testículo/metabolismo
5.
Dev Comp Immunol ; 48(1): 204-9, 2015 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-25451300

RESUMEN

ADP-ribosylation factors (Arfs) are small GTP-binding proteins that have an essential function in intracellular trafficking and organelle structure. To date, little information is available on the Arfs in the economically important giant freshwater prawn Macrobrachium rosenbergii and their relationship to viral infection. Here we identified two Arf genes from M. rosenbergii (MrArf1 and MrArf2) for the first time. Phylogenetic analysis showed that MrArf1, together with MjArf1 from shrimp Marsupenaeus japonicus belonged to Class I Arfs. By contrast, MrArf2 didn't not match any of the Arfs classes of I/II/III, although it could be clustered with an Arf protein from M. japonicas called MjArfn, which may represent an analog of the Arf. MrArf1 was ubiquitously expressed in all the examined tissues, with the highest transcription level in the hepatopancreas, whereas MrArf2 was only highly expressed in the hepatopancreas and exhibited very low levels in the heart, stomach, gills and intestine. The expression level of MrArf1 in the gills was down-regulated post 24 h WSSV challenge, and reached the maximal level at 48 h. MrArf1 in the hepatopancreas went up from 24 to 48 h WSSV challenge. MrArf2 transcript in the gill also went down at 24 h and then was upregulated at 48 h WSSV challenge. MrArf2 increased significantly in the hepatopancreas 24 h after infection and then went down at 48 h WSSV challenge. RNAi results showed that knockdown of MrArf1 or MrArf2 could inhibit the expression of the envelope protein gene vp28 of the WSSV. So, it could be speculated that MrArf1 and MrArf2 might play important roles in the innate immune system against WSSV infection.


Asunto(s)
Factor 1 de Ribosilacion-ADP/genética , Palaemonidae/inmunología , Virus del Síndrome de la Mancha Blanca 1/inmunología , Factor 1 de Ribosilacion-ADP/biosíntesis , Factor 1 de Ribosilacion-ADP/inmunología , Secuencia de Aminoácidos , Animales , Clonación Molecular , Regulación de la Expresión Génica/inmunología , Palaemonidae/virología , Interferencia de ARN , ARN Interferente Pequeño , Alineación de Secuencia , Homología de Secuencia , Proteínas del Envoltorio Viral/antagonistas & inhibidores , Proteínas del Envoltorio Viral/biosíntesis
6.
Dev Comp Immunol ; 46(2): 255-66, 2014 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-24796868

RESUMEN

L-type lectins contain a leguminous lectin domain and bind to high-mannose type oligosaccharides. In the secretory pathway, L-type lectins play crucial functions in the trafficking, sorting, and targeting of maturing glycoproteins. This study identified two novel L-type lectins, designated as EsERGIC-53 and EsVIP36, from the Chinese mitten crab Eriocheir sinensis. The complete nucleotide sequence of ERGIC-53 cDNA was 1955 bp, containing a 1506 bp open reading frame (ORF) encoding a putative protein of 501 deduced amino acids. The full-length cDNA of VIP36 was 3474 bp with a 984 bp ORF encoding a 327-amino acid peptide. The deduced ERGIC-53 and VIP36 proteins contained a putative signal peptide and an L-type lectin-like domain. Phylogenetic analysis showed that ERGIC-53 and VIP36 belonged to different clades of L-type lectin family. Reverse transcription PCR showed that ERGIC-53 and VIP36 were expressed in all tested tissues. Quantitative real-time RT-PCR analysis revealed that ERGIC-53 and VIP36 transcripts in hepatopancreas were significantly induced at various time points after infection with lipopolysaccharide (LPS), peptidoglycan (PGN), Staphylococcus aureus, Vibrio parahaemolyticus, and Aeromonas hydrophila. A bacterium-binding experiment showed that both ERGIC-53 and VIP36 could bind to different microbes. Sugar binding assay revealed that these lectins could also bind to the glycoconjugates of bacteria surface, such as LPS, PGN, d-Mannose, and N-Acetyl-d-mannosamine. Moreover, these two L-type lectins agglutinated bacteria in a calcium-dependent manner, and both exerted the ability of facilitating the clearance of injected bacteria V. parahaemolyticus in the crab. Our results suggested that ERGIC-53 and VIP36 functioned as pattern recognition receptors in the immune system of E. sinensis.


Asunto(s)
Proteínas de Artrópodos/genética , Braquiuros/genética , Lectinas/genética , Aglutinación , Secuencia de Aminoácidos , Animales , Antibacterianos/farmacología , Proteínas de Artrópodos/biosíntesis , Proteínas de Artrópodos/química , Proteínas de Artrópodos/farmacología , Bacillus subtilis/efectos de los fármacos , Secuencia de Bases , Braquiuros/inmunología , Braquiuros/microbiología , Clonación Molecular , Secuencia Conservada , Expresión Génica , Interacciones Huésped-Patógeno , Inmunidad Innata , Lectinas/biosíntesis , Lectinas/química , Lectinas/farmacología , Lipopolisacáridos/química , Datos de Secuencia Molecular , Especificidad de Órganos , Filogenia , Unión Proteica , Estructura Terciaria de Proteína , Staphylococcus aureus/efectos de los fármacos , Staphylococcus aureus/inmunología , Vibrio parahaemolyticus/efectos de los fármacos
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