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Marine Drugs
Special Issues
The Road from DNA to Metabolomics Using a Comprehensive Strategy...
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The Road from DNA to Metabolomics Using a Comprehensive Strategy for the Discovery of New Marine Microbial Metabolites

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (16 October 2022) | Viewed by 5820

Special Issue Editor

Dr. Zeinab Khalil

E-Mail Website
Guest Editor
Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072, Australia
Interests: biosynthesis; microbial; natural product biodiscovery; gene clusters; multi-drug resistant pathogens
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Microbial natural products are a potential source of new drugs, leading to the protection of human and animal health against various pathogens. Therefore, the identification of strategies to detect new secondary metabolites is crucial to finding new drug leads. Advances in full-genome sequencing, transcriptomics and proteomics can provide a valuable tool to determine the metabolomic capability of these microbes (fungi and bacteria). In this Special Issue, we aim to incorporate valuable bioinformatics and computational tools through a step-by-step process to investigate marine microbial gene clusters, targeting the discovery of new marine drug leads.

Dr. Zeinab Khalil
Guest Editor

Manuscript Submission Information

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

  • microbial natural products
  • new drugs
  • genome sequencing
  • transcriptomics
  • proteomics
  • fungi
  • bacteria
  • bioinformatics
  • computational tools
  • gene clusters

Published Papers (2 papers)

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Research

11 pages, 2808 KiB  
Article
Genome Mining of α-Pyrone Natural Products from Ascidian-Derived Fungus Amphichordafelina SYSU-MS7908
by Siwen Yuan, Litong Chen, Qilin Wu, Minghua Jiang, Heng Guo, Zhibo Hu, Senhua Chen, Lan Liu and Zhizeng Gao
Mar. Drugs 2022, 20(5), 294; https://doi.org/10.3390/md20050294 - 27 Apr 2022
Cited by 6 | Viewed by 2142
Abstract
Culturing ascidian-derived fungus Amphichorda felina SYSU-MS7908 under standard laboratory conditions mainly yielded meroterpenoid, and nonribosomal peptide-type natural products. We sequenced the genome of Amphichorda felina SYSU-MS7908 and found 56 biosynthetic gene clusters (BGCs) after bioinformatics analysis, suggesting that the majority of those BGCSs [...] Read more.
Culturing ascidian-derived fungus Amphichorda felina SYSU-MS7908 under standard laboratory conditions mainly yielded meroterpenoid, and nonribosomal peptide-type natural products. We sequenced the genome of Amphichorda felina SYSU-MS7908 and found 56 biosynthetic gene clusters (BGCs) after bioinformatics analysis, suggesting that the majority of those BGCSs are silent. Here we report our genome mining effort on one cryptic BGC by heterologous expression in Aspergillus oryzae NSAR1, and the identification of two new α-pyrone derivatives, amphichopyrone A (1) and B (2), along with a known compound, udagawanone A (3). Anti-inflammatory activities were performed, and amphichopyrone A (1) and B (2) displayed potent anti-inflammatory activity by inhibiting nitric oxide (NO) production in RAW264.7 cells with IC50 values 18.09 ± 4.83 and 7.18 ± 0.93 μM, respectively. Full article
(This article belongs to the Special Issue The Road from DNA to Metabolomics Using a Comprehensive Strategy for the Discovery of New Marine Microbial Metabolites)
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16 pages, 2543 KiB  
Article
Evaluation of a Thermophilic, Psychrostable, and Heavy Metal-Resistant Red Sea Brine Pool Esterase
by Shimaa F. Ahmed, Rehab Z. Abdallah and Rania Siam
Mar. Drugs 2022, 20(5), 274; https://doi.org/10.3390/md20050274 - 19 Apr 2022
Cited by 2 | Viewed by 3227
Abstract
Lipolytic enzymes catalyze the hydrolysis and synthesis of ester compounds. They are valuable in the pulp, food, and textile industries. This study aims to comprehensively evaluate the extreme properties of a hormone-sensitive lipase (EstATII-TM) isolated from the Red Sea Atlantis II brine pool. [...] Read more.
Lipolytic enzymes catalyze the hydrolysis and synthesis of ester compounds. They are valuable in the pulp, food, and textile industries. This study aims to comprehensively evaluate the extreme properties of a hormone-sensitive lipase (EstATII-TM) isolated from the Red Sea Atlantis II brine pool. EstATII-TM was cloned, expressed, and its biochemical activities were assessed under different conditions. EstATII-TM catalytic properties and resistance to different metal ions were compared to commercial thermophilic esterases under different temperatures. Phylogenetically, EstATII-TM was assigned to the GDSAG motif subfamily of hormone-sensitive lipase. The optimal enzyme activity was evident at a temperature of 30 °C and pH 7–8. The enzyme retained 84.9% of its activity at 0.5 M NaCl. EstATII-TM maintained 93% to 97% activity at −40 and −20 °C, respectively. EstATII-TM activity was significantly enhanced, up to 10-fold, at temperatures ranging from 45 to 65 °C in the presence of 1 mM Cu2+, Cd2+, Ba2+, Mn2+, and Zn2+. EstATII-TM showed superior catalytic activity and resistance-to/enhancement-by metal ions compared to two commercial thermophilic esterases. The Red Sea Atlantis II brine EstATII-TM is characterized by tolerance to high temperatures, stability to hot and cold conditions, as well as toxic heavy metal contamination, making it an ideal candidate for industrial processes. Full article
(This article belongs to the Special Issue The Road from DNA to Metabolomics Using a Comprehensive Strategy for the Discovery of New Marine Microbial Metabolites)
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