Transcriptomic and proteomic analyses of splenic immune mechanisms of rainbow trout (Oncorhynchus mykiss) infected by Aeromonas salmonicida subsp. salmonicida

Long, Meng; Zhao, Juan; Li, Tongtong; Tafalla, Carolina; Zhang, Qianqian; Wang, Xiehao; Gong, Xiaohua; Shen, Zhixin; Li, Aihua

doi:10.1016/j.jprot.2015.03.031

Cited by 84 publications

(44 citation statements)

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“…The number of kidney proteins is consistent with that reported in other fish species: 385 proteins were identified in the kidney from zebrafish; 4009 proteins in the kidney from Atlantic salmon . However, the number of spleen proteins (2542 proteins) was much higher in our study than reported by Long et al, where they found 1447 proteins in the spleen of rainbow trout in a study applying iTRAQ labeling for quantification. The overall list of identified proteins, protein score, confident peptides, sequence coverage, and ambiguous accessions to each protein is provided in Tables S1 and S2, Supporting Information.…”

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confidence: 82%

“…There is limited knowledge about detailed proteome of rainbow trout lymphoid organs. Only differential protein expression profiles in the spleen of rainbow trout have been examined to investigate the immune mechanisms against Aeromonas salmonicida infection . To understand lymphoid organs functions and disease, it is important to define the molecular constituents of the various compartments of the head kidney and spleen proteome profiles of rainbow trout.…”

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Proteome Profiles of Head Kidney and Spleen of Rainbow Trout (Oncorhynchus Mykiss)

et al. 2018

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The head kidney and spleen are major lymphoid organs of the teleost fish. The authors identify proteome profiles of head kidney and spleen of rainbow trout (Oncorhynchus mykiss) using a shotgun proteomic approach. Gene ontology annotation of proteins is predicted using bioinformatic tools. This study represents detailed proteome profiles of head kidney and spleen of rainbow trout, with a total of 3241 and 2542 proteins identified, respectively. It is found that lymphoid organs are equipped with a variety of functional proteins related to defense, receptor, signal transduction, antioxidant, cytoskeleton, transport, binding, and metabolic processes. The identified proteome profiles will serve as a template for understanding lymphoid organ functions in salmonids and will increase the amount of spectra information of rainbow trout proteins in the public data repository PRIDE. This data can be accessed via ProteomeXchange with identifiers PXD008473 and PXD008478.

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confidence: 99%

Proteome Profiles of Head Kidney and Spleen of Rainbow Trout (Oncorhynchus Mykiss)

et al. 2018

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“…Proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure and distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP-dependent process [26]. We found that 8 up-regulated proteins enriched in the proteasome pathway between 60-d hibernation group and pre-hibernation group (26S proteasome non-ATPase regulatory subunit 4, 26S protease regulatory subunit 10B, 26S protease regulatory subunit 6A, 26S protease regulatory subunit 6B isoform X1, proteasome subunit alpha type-6, proteasome subunit alpha type-5, proteasome subunit alpha type-3 isoform X1, proteasome subunit beta type-6 isoform X1, Fig.…”

Section: Resultsmentioning

confidence: 99%

iTRAQ-based proteomic analysis of myofibrillar contents and relevant synthesis and proteolytic proteins in soleus muscle of hibernating Daurian ground squirrels (Spermophilus dauricus)

et al. 2016

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BackgroundDaurian ground squirrels (Spermophilus dauricus) deviate from significant increase of protein catabolism and loss of myofibrillar contents during long period of hibernation inactivity.MethodsHere we use iTRAQ based quantitative analysis to examine proteomic changes in the soleus of squirrels in pre-hibernation, hibernation and post-hibernation states. The total proteolysis rate of soleus was measured by the release of the essential amino acid tyrosine from isolated muscles. Immunofluorescent analysis was used to determine muscle fiber cross-sectional area. Western blot was used for the validation of the quantitative proteomic analysis.ResultsThe proteomic responses to hibernation had a 0.4- to 0.8-fold decrease in the myofibrillar contractile protein levels of myosin-3, myosin-13 and actin, but a 2.1-fold increase in myosin-2 compared to pre-hibernation group. Regulatory proteins such as troponin C and tropomodulin-1 were 1.4-fold up-regulated and 0.7-fold down-regulated, respectively, in hibernation compared to pre-hibernation group. Moreover, 10 proteins with proteolytic function in hibernation, which was less than 14 proteins in the post-hibernation group, were up-regulated relative to the pre-hibernation group. The total proteolysis rates of soleus in hibernation and post-hibernation groups were significantly inhibited as compared with pre-hibernation group.ConclusionThese findings suggest that the myofibrillar remodeling and partial suppression of myofibrillar proteolysis were likely responsible for preventing skeletal muscle atrophy during prolonged disuse in hibernation. This is the first study where the myofibrillar contents and relevant synthesis and proteolytic proteins in slow soleus was discussed based on proteomic investigation performed on wild Daurian ground squirrels. Our results lay the foundation for further research in preventing disuse-induced skeletal muscle atrophy in mammals.Electronic supplementary materialThe online version of this article (doi:10.1186/s12953-016-0105-x) contains supplementary material, which is available to authorized users.

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“…Interest at the level of gene and protein function will provide a more comprehensive understanding of a species’ biology and its response/adaptation to the environment. The main areas of research that have adhered to this technology have been aquaculture for improving fish health and nutrition, welfare assessment and stress reduction, diseases and the use of antibiotics and vaccines, aquatic toxicology, and the identification of major environmental threats and the mode of action (MOA) of water contaminants [52,53,54]; developmental biology and reproduction [55,56,57]; and physiology and immune mechanisms in selected wildlife and commercial species [58,59,60,61]. The conventional proteomic techniques such as quantitative 2DE and 2D-DIGE in combination with MS have been the most used to address specific proteomic questions raised in aquatic sciences.…”

Section: Top-down Proteomics In Aquatic Sciencesmentioning

confidence: 99%

Top-Down Proteomics and Farm Animal and Aquatic Sciences

Campos

Almeida

2016

Proteomes

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Proteomics is a field of growing importance in animal and aquatic sciences. Similar to other proteomic approaches, top-down proteomics is slowly making its way within the vast array of proteomic approaches that researchers have access to. This opinion and mini-review article is dedicated to top-down proteomics and how its use can be of importance to animal and aquatic sciences. Herein, we include an overview of the principles of top-down proteomics and how it differs regarding other more commonly used proteomic methods, especially bottom-up proteomics. In addition, we provide relevant sections on how the approach was or can be used as a research tool and conclude with our opinions of future use in animal and aquatic sciences.

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Transcriptomic and proteomic analyses of splenic immune mechanisms of rainbow trout (Oncorhynchus mykiss) infected by Aeromonas salmonicida subsp. salmonicida

Cited by 84 publications

References 71 publications

Proteome Profiles of Head Kidney and Spleen of Rainbow Trout (Oncorhynchus Mykiss)

Proteome Profiles of Head Kidney and Spleen of Rainbow Trout (Oncorhynchus Mykiss)

iTRAQ-based proteomic analysis of myofibrillar contents and relevant synthesis and proteolytic proteins in soleus muscle of hibernating Daurian ground squirrels (Spermophilus dauricus)

Top-Down Proteomics and Farm Animal and Aquatic Sciences

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