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Special Issue "Marine Proteomics in Exploring Bioactive Peptides and Proteins"

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Laboratory of Biology of Aquatic Organisms and Ecosystems, Université de Caen Normandie, Caen, France
Interests: transcriptomics; peptidomic; proteomics; immunity; neuropeptides; antimicrobial peptides
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Dear Colleagues,

The diversity of marine organisms from coastal areas to the deep sea represents a source of new bioactive molecules. With new technologies and new approaches developed in omics and especially in proteomics, the characterization of new proteins or peptides is booming. These new proteins or peptides present in marine organisms play a role in the structure and/or function of these organisms but may represent a new source of drugs. Thus, it is possible from marine species—including venomous species not studied at all or studied little—to discover new antimicrobial peptides, new toxins that could constitute new antibiotics, analgesics, and anesthetics for human or animal health. Among peptides, neuropeptides also play an essential role in major physiological functions such as reproduction and nutrition and also constitute a source of drugs very often unexplored.

I invite researchers from different disciplines including biology, physiology, chemistry, biochemistry, medical science, and other fields to consider making a contribution to this Special Issue on “Marine Proteomics in Exploring Bioactive Peptides and Proteins” and to highlight the contributions of proteomics to unconventional marine models.

Dr. Céline Zatylny-Gaudin
Guest Editor

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Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

marine proteomics
marine bioactive peptides
marine natural products
marine drugs
marine proteins
marine peptides
marine organisms
marine antimicrobial peptides

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Research

Open AccessArticle

Functional Diversification of Oyster Big Defensins Generates Antimicrobial Specificity and Synergy against Members of the Microbiota

Mar. Drugs 2022, 20(12), 745; https://doi.org/10.3390/md20120745 - 26 Nov 2022

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Abstract

Big defensins are two-domain antimicrobial peptides (AMPs) that have highly diversified in mollusks. Cg-BigDefs are expressed by immune cells in the oyster Crassostrea gigas, and their expression is dampened during the Pacific Oyster Mortality Syndrome (POMS), which evolves toward fatal bacteremia. We evaluated whether Cg-BigDefs contribute to the control of oyster-associated microbial communities. Two Cg-BigDefs that are representative of molecular diversity within the peptide family, namely Cg-BigDef1 and Cg-BigDef5, were characterized by gene cloning and synthesized by solid-phase peptide synthesis and native chemical ligation. Synthetic peptides were tested for antibacterial activity against a collection of culturable bacteria belonging to the oyster microbiota, characterized by 16S sequencing and MALDI Biotyping. We first tested the potential of Cg-BigDefs to control the oyster microbiota by injecting synthetic Cg-BigDef1 into oyster tissues and analyzing microbiota dynamics over 24 h by 16S metabarcoding. Cg-BigDef1 induced a significant shift in oyster microbiota β-diversity after 6 h and 24 h, prompting us to investigate antimicrobial activities in vitro against members of the oyster microbiota. Both Cg-BigDef1 and Cg-BigDef5 were active at a high salt concentration (400 mM NaCl) and showed broad spectra of activity against bacteria associated with C. gigas pathologies. Antimicrobial specificity was observed for both molecules at an intra- and inter-genera level. Remarkably, antimicrobial spectra of Cg-BigDef1 and Cg-BigDef5 were complementary, and peptides acted synergistically. Overall, we found that primary sequence diversification of Cg-BigDefs has generated specificity and synergy and extended the spectrum of activity of this peptide family. Full article

(This article belongs to the Special Issue Marine Proteomics in Exploring Bioactive Peptides and Proteins)

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Open AccessArticle

Structural and Functional Characterization of Orcokinin B-like Neuropeptides in the Cuttlefish (Sepia officinalis)

Maxime Endress

Céline Zatylny-Gaudin

and

Mar. Drugs 2022, 20(8), 505; https://doi.org/10.3390/md20080505 - 04 Aug 2022

Cited by 1 | Viewed by 1145

Abstract

The cuttlefish (Sepia officinalis) is a Cephalopod mollusk that lives in the English Channel and breeds in coastal spawning grounds in spring. A previous work showed that the control of egg-laying is monitored by different types of regulators, among which neuropeptides play a major role. They are involved in the integration of environmental cues, and participate in the transport of oocytes in the genital tract and in the secretion of capsular products. This study addresses a family of neuropeptides recently identified and suspected to be involved in the control of the reproduction processes. Detected by mass spectrometry and immunocytochemistry in the nerve endings of the accessory sex glands of the females and ovary, these neuropeptides are also identified in the hemolymph of egg-laying females demonstrating that they also have a hormone-like role. Released in the hemolymph by the sub-esophageal mass, a region that innervates the genital tract and the neurohemal area of the vena cava, in in vitro conditions these neuropeptides modulated oocyte transport and capsular secretion. Finally, in silico analyses indicated that these neuropeptides, initially called FLGamide, had extensive structural homology with orcokinin B, which motivated their name change. Full article

(This article belongs to the Special Issue Marine Proteomics in Exploring Bioactive Peptides and Proteins)

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Special Issue "Marine Proteomics in Exploring Bioactive Peptides and Proteins"

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