Apolipoprotein A1 in channel catfish: Transcriptional analysis, antimicrobial activity, and efficacy as plasmid DNA immunostimulant against Aeromonas hydrophila infection

Pridgeon, Julia W.; Klesius, Phillip H.

doi:10.1016/j.fsi.2013.07.028

Cited by 31 publications

(28 citation statements)

References 30 publications

(32 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Apo5 and Apo6 are highly related peptides; nested fragments of a purported apolipoprotein. Apolipoproteins have antimicrobial activity against a variety of pathogenic bacteria [9–14] (see Discussion). A1P is the C-terminal fragment of alpha-1-proteinase inhibitor of the serpin family; this protease inhibitor has broad protease inhibiting activity, as well as immunomodulatory effects [15].…”

Section: Introductionmentioning

confidence: 99%

Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii

et al. 2016

View full text Add to dashboard Cite

BackgroundOur group has developed a new process for isolating and identifying novel cationic antimicrobial peptides from small amounts of biological samples. Previously, we identified several active antimicrobial peptides from 100 μl of plasma from Alligator mississippiensis. These peptides were found to have in vitro antimicrobial activity against Pseudomonas aeruginosa and Staphylococcus aureus. In this work, we further characterize three of the novel peptides discovered using this process: Apo5, Apo6, and A1P.ResultsWe examined the activity of these peptides against multi-drug resistant strains and clinical isolates of common human pathogens. We investigated their structural characteristics using circular dichroism and tested for membrane disruption and DNA binding. These peptides were found to have strong in vitro activity against multi-drug resistant and clinically isolated strains of S. aureus, Escherichia coli, P. aeruginosa, and Acinetobacter baumannii. Apo5 and Apo6, peptides derived from alligator apolipoprotein C-1, depolarized the bacterial membrane. A1P, a peptide from the serpin proteinase inhibitor, did not permeabilize membranes. Performing circular dichroism analysis, Apo5 and Apo6 were found to be predominantly helical in SDS and TFE buffer, while A1P has significantly different structures in phosphate buffer, SDS, and TFE. None of these peptides were found to be hemolytic to sheep red blood cells or significantly cytotoxic up to 100 μg/ml after 24 h exposure.ConclusionsOverall, we suggest that Apo5 and Apo6 have a different mode of action than A1P, and that all three peptides make promising candidates for the treatment of drug-resistant bacteria, such as A. baumannii.

show abstract

Section: Introductionmentioning

confidence: 99%

Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii

et al. 2016

View full text Add to dashboard Cite

show abstract

“…The expression of Ec-ApoA-I was detected in all tested tissues, with the predominant expression in the liver and intestine. Ubiquitous expression of ApoA-1 in different tissues has been previously reported in various fish species, including ayu (Plecoglossus altivelis) [14], rainbow trout (O. mykiss) [25] and channel catfish (I. punctatus) [18]. Although the tissue expression pattern of ApoA-I mRNA differs among fish species [14], the liver and the intestine typically constitute the major sites of ApoA-I gene expression in most teleosts [14,38], which coincides with the major sites in mammals and birds [39,40].…”

Section: Discussionmentioning

confidence: 85%

“…Of all collected tissues, ApoA-I in skin, anterior kidney, and blood were significantly more up-regulated by the infection of A. hydrophila by bath immersion [18]. Significant upregulation of ApoA-I in blood post vaccination with heat-killed Listonella anguillarum by intraperitoneal injection has been reported in Atlantic cod (Gadus morhua) [44].…”

Section: Discussionmentioning

confidence: 86%

“…Although ApoA-I from other fish have been reported to possess bacteriolyticactivity [18], Ec-ApoA-I was not reported previously. Ec-ApoA-I contained the conserved apolipoprotein domain, suggesting that Ec-ApoA-I might possess bacteriolyticactivity.…”

Section: Discussionmentioning

confidence: 87%

“…For example, human ApoA-I has antiviral activity against Herpes Simplex Virus (HSV), human immunodeficiency virus (HIV), and xenotropic murine virus [21e23]. Teleostean ApoA-I isolated from carp (Cyprinus carpio), rainbow trout (Oncorhynchus mykiss), Channel Catfish (Ictalurus punctatus) and striped bass (Morone saxatilis) demonstrates in vitro antibacterial activity [2,18,24,25].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Isolation and function analysis of apolipoprotein A-I gene response to virus infection in grouper

Wei

Gao

Zhang

et al. 2015

Fish & Shellfish Immunology

View full text Add to dashboard Cite

Skin mucus proteome map of European sea bass (Dicentrarchus labrax)

et al. 2015

View full text Add to dashboard Cite

Abbreviations: AFP, antifreeze proteins; APOA1, Apolipoprotein A1; ASC, apoptosisassociated speck-like protein containing a caspase recruitment domain; C3, complement component 3; CALM, calmodulin; CALR, calreticulin; CASP, caspase; cDNA, complementary DNA; ERp57,endoplasmic reticulum protein 57; FBL, fucose-binding lectin; H1/4, histone H1/H4; IL1B, interleukin 1-beta; LEI, leukocyte elastase inhibitor; LYZ, lysozyme; qPCR, real-time PCR; PRDX, peroxiredoxin; SOD superoxide dismutase; TF, transferrin; WAP65, warm temperature acclimation related 65 kDa protein; www.proteomics-journal.com Page 2 ProteomicsThis article is protected by copyright. All rights reserved.Keywords: European sea bass (Dicentrarchus labrax), mucosal immunity, proteome, skin mucus, transcript profile. AbstractSkin mucus is the first barrier of fish defence. Proteins from skin mucus of European sea bass (Dicentrarchus labrax) were identified by 2DE followed by LC-MS/MS. From all the identified proteins in the proteome map, we focus on the proteins associated with several immune pathways in fish. Furthermore, the qPCR transcript levels in skin are shown. Proteins found include apolipoprotein A1, calmodulin, complement C3, fucose-binding lectin, lysozyme and several caspases. To our knowledge, this is the first skin mucus proteome study and further transcriptional profiling of the identified proteins done on this bony fish species.This not only contributes knowledge on the routes involved in mucosal innate immunity, but also establishes a non-invasive technique based on locating immune markers with a potential use for prevention and/or diagnosis of fish diseases.www.proteomics-journal.com Page 3 ProteomicsThis article is protected by copyright. All rights reserved. Statement of significance of the studyThe skin mucus is the first defence barrier of teleost fish; together with the skin, it protects the animal from pathogens, potential harmful chemicals and physical factors in the water where it is constantly submerged. This study identifies for the first time the main proteins in the skin mucus of European sea bass (Dicentrarchus labrax). In particular, we identify immune relevant proteins. The presence of RNA of the immune relevant genes in skin indicates that the proteins could be synthesised in the skin itself.

show abstract

Apolipoprotein A1 in channel catfish: Transcriptional analysis, antimicrobial activity, and efficacy as plasmid DNA immunostimulant against Aeromonas hydrophila infection

Cited by 31 publications

References 30 publications

Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii

Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii

Isolation and function analysis of apolipoprotein A-I gene response to virus infection in grouper

Skin mucus proteome map of European sea bass (Dicentrarchus labrax)

Contact Info

Product

Resources

About