Molecular characterization of two isoforms of piscidin 4 from the hybrid striped bass (Morone chrysops × Morone saxatilis)

Salger, Scott A.; Reading, Benjamin J.; Baltzegar, David A.; Sullivan, Craig V.; Noga, Edward J.

doi:10.1016/j.fsi.2010.10.009

Cited by 41 publications

(29 citation statements)

References 26 publications

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“…The smaller of these products was uniquely observed in the genomic DNA of white bass (GenBank; KX231312) and the larger present in striped bass (Genbank; KX232424) (Fig 3) indicating that two distinct orthologues of piscidin 5 are present in the hybrid striped bass genome. The open reading frame of the smaller piscidin 5 gene in hybrid striped bass and white bass corresponds to the previously published piscidin 5 gene transcript sequence [13], whereas the larger hybrid striped bass and striped bass piscidin 5 gene codes for an incomplete peptide (S2 Fig). …”

Section: Resultsmentioning

confidence: 62%

“…White bass piscidins 4 and 5 of Class II have similar antibacterial and antiprotozoal activities (Tables 3 and 4), suggesting that the active region of the peptide is the α-helical N-terminal region that is highly conserved between the two piscidin forms (Fig 2) [13]. The N-terminal region has been shown to intercalate into the phospholipid bilayer of membranes when analyzing tryptophan quenching data from striped bass piscidin 4 [48], which also has a similar structure.…”

Section: Discussionmentioning

confidence: 99%

“…Further research into the diversity and evolution of host-defense peptides may lead to a greater understanding of their functions, thus aiding research into potential therapeutic applications. We have previously reported the complete coding sequence and preliminary characterization of two novel piscidins from hybrid striped bass [13]. Here, we present information on other related host-defense peptides, along with a new piscidin classification scheme.…”

Section: Introductionmentioning

confidence: 99%

“…One type of host-defense peptides are α-helical, amphipathic polypeptides [9] and a sub-group of these peptides is the piscidins which range from 18 to 46 amino acid residues in length [12–13]. Originally isolated as peptides from the striped bass ( Morone saxatilis ), white bass ( M .…”

Section: Introductionmentioning

confidence: 99%

“…The amino acid sequence of chrysophsins, antimicrobial peptides isolated from red sea bream ( Chrysophrys major ), a member of the family Sparidae, also are similar to the piscidins [20]. Piscidin gene transcripts have been cloned as cDNAs and characterized in striped bass and white bass [15], the hybrid striped bass [13], European seabass ( Dicentrarchus labrax ) [21], mandarin fish ( Siniperca chuatsi ) [22], Nile tilapia ( Oreochromis niloticus ) [23–24] and Atlantic cod ( Gadus morhua ) [25]. Genomic evidence suggests that the pleurocidins, found in many flatfish species, also are members of the piscidin family [22], as may be epinecidins of the grouper, Epinephelus coioides [26].…”

Section: Introductionmentioning

confidence: 99%

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A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes

et al. 2016

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Conventional antibiotics and other chemical-based drugs are currently one of the most common methods used to control disease-related mortality in animal agriculture. Use of the innate immune system to decrease disease related mortalities is a novel alternative to conventional drugs. One component of the innate immune system is the host-defense peptides, also known as antimicrobial peptides. Host-defense peptides are typically small, amphipathic, α-helical peptides with a broad-spectrum of action against viral, bacterial, fungal, and/or protozoal pathogens. Piscidins are host-defense peptides first discovered in the hybrid striped bass (white bass, Morone chrysops, x striped bass, M. saxatilis). In this paper we identify four new piscidin isoforms in the hybrid striped bass and describe their tissue distributions. We also determine the progenitor species of origin of each piscidin (orthology) and propose a revised nomenclature for this newly described piscidin family based on a three class system. The Class I piscidins (22 amino acids in length; striped bass and white bass piscidin 1 and piscidin 3) show broad-spectrum activity against bacteria and ciliated protozoans, while the Class III piscidins (55 amino acids in length; striped bass and white bass piscidin 6 and striped bass piscidin 7) primarily show anti-protozoal activity. The Class II piscidins (44–46 amino acids in length; striped bass and white bass piscidin 4 and white bass piscidin 5) have a level of activity against bacteria and protozoans intermediate to Classes I and III. Knowledge of piscidin function and activity may help in the future development of disease-resistant lines of striped bass and white bass that could be used to produce superior hybrids for aquaculture.

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Section: Resultsmentioning

confidence: 62%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes

et al. 2016

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Acidophilic granulocytes in the gills of gilthead seabream Sparus aurata: evidence for their responses to a natural infection by a copepod ectoparasite

et al. 2013

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Immunohistochemical and ultrastructural studies were conducted on the gills of gilthead seabream, Sparus aurata L., naturally infected with the copepod ectoparasite Ergasilus lizae (Krøyer, 1863) in order to assess pathology and the host immune cell response. Gills of 56 gilthead seabream were screened for ectoparasites; 36 specimens (64.3%) harbored E. lizae. Intensity of infection was 32.7 ± 8.7 (mean ± SE). Pathological alterations to the gills of the host were more pronounced in close proximity to the copepod site of attachment. The parasite attached to the gills by means of its modified second antennae, occluded the arteries, provoked epithelial hyperplasia and hemorrhages and most often caused lamellar disruption. Numerous granular cells were encountered near the site of E. lizae attachment. In both infected and uninfected gills, the granular cells lay within the filaments and frequently occurred within the connective tissue inside and outside the blood vessels of the filaments. The type of granular cell was identified by immunohistochemical staining by using the monoclonal antibody G7 (mAb G7), which specifically recognizes acidophilic granulocytes (AGs) of S. aurata and with an anti-histamine antibody (as a marker for mast cells, MCs) on sections from 13 uninfected gills and 21 parasitized gills. The use of mAb G7 revealed that, in gills harboring copepods, the number of G7-positive cells (i.e., AGs; 32.9 ± 3.9, mean number of cells per 45,000 μm2 ± SE) was significantly higher than the density of the same cells in uninfected gills (15.3 ± 3.8; ANOVA, P < 0.05). Few histamine-positive granular cells (i.e., MCs) were found in the uninfected and parasitized gills. Here, we show, for the first time in S. aurata infected gills, that AGs rather than MCs are recruited and involved in the response to E. lizae infection in seabream.

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Piscidin, Fish Antimicrobial Peptide: Structure, Classification, Properties, Mechanism, Gene Regulation and Therapeutical Importance

Raju

Sarkar

Kumar

et al. 2020

Int J Pept Res Ther

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Molecular characterization of two isoforms of piscidin 4 from the hybrid striped bass (Morone chrysops × Morone saxatilis)

Cited by 41 publications

References 26 publications

A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes

A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes

Acidophilic granulocytes in the gills of gilthead seabream Sparus aurata: evidence for their responses to a natural infection by a copepod ectoparasite

Piscidin, Fish Antimicrobial Peptide: Structure, Classification, Properties, Mechanism, Gene Regulation and Therapeutical Importance

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