Plastid engineering of a marine alga, Nannochloropsis gaditana, for co‐expression of two recombinant peptides

Background: Bacteriocins (Bac1, Bac2, and Bac3) from Weissella confusa MBF8-1, weissellicin- MBF, have been reported as potential alternative substances as well as complements to the existing antibiotics against many antimicrobial-resistant pathogens. Previously, the genes encoded in the large plasmid, pWcMBF8-1, and the spermicidal activity of their synthetic peptides, originally discovered Indonesia, have been studied. Three synthetic bacteriocins peptides of this weissellicin-MBF have been reported for their potential activities, i.e. antibacterial and spermicidal. Objective: The aim of this study was to construct the recombinant Bacteriocin (r-Bac) genes, as well as to investigate the gene expressions and their functional analysis. Method: Here, the recombinant Bacteriocin (r-Bac) genes were constructed and the recombinant peptides (r-Bac1, r-Bac2, and r-Bac3) in B. subtilis DB403 cells were produced on a large scale. After purification, using the His-tag affinity column, their potential bioactivities were measured as well as their antibacterial minimum inhibitory concentrations against Leuconostoc mesenteroides and Micrococcus luteus, were determined. Results: Pure His-tag-recombinant Bac1, Bac2, and Bac3 were obtained and they could inhibit the growth of L. mesenteroides and M. luteus. Conclusion: The recombinant bacteriocin could be obtained although with weak activity in inhibiting gram-positive bacterial growth.

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Polygalacto-fucopyranose from marine alga as a prospective antihypertensive lead

International Journal of Biological Macromolecules ◽

10.1016/j.ijbiomac.2021.04.140 ◽

2021 ◽

Author(s):

Gangadhar Surabhi ◽

Shubhajit Dhara ◽

Anusree Maneesh ◽

Kajal Chakraborty ◽

Lokanatha Valluru ◽

...

Keyword(s):

Marine Alga

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A PEPTIDE FROM A MARINE ALGA

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)56595-9 ◽

1949 ◽

Vol 181 (2) ◽

pp. 719-729

Author(s):

Charles A. Dekker ◽

David. Stone ◽

Joseph S. Fruton

Keyword(s):

Marine Alga

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Identification, heterologous production and bioactivity of lentinulin A and dendrothelin A, two natural variants of backbone N-methylated peptide macrocycle omphalotin A

Scientific Reports ◽

10.1038/s41598-021-83106-2 ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Emmanuel Matabaro ◽

Hannelore Kaspar ◽

Paul Dahlin ◽

Daniel L. V. Bader ◽

Claudia E. Murar ◽

...

Keyword(s):

Natural Products ◽

Lentinula Edodes ◽

Gene Clusters ◽

Biosynthetic Gene Cluster ◽

Precursor Protein ◽

Fungal Genome ◽

Homologous Gene ◽

C Terminus ◽

Natural Variants ◽

Recombinant Peptides

AbstractBackbone N-methylation and macrocyclization improve the pharmacological properties of peptides by enhancing their proteolytic stability, membrane permeability and target selectivity. Borosins are backbone N-methylated peptide macrocycles derived from a precursor protein which contains a peptide α-N-methyltransferase domain autocatalytically modifying the core peptide located at its C-terminus. Founding members of borosins are the omphalotins from the mushroom Omphalotus olearius (omphalotins A-I) with nine out of 12 L-amino acids being backbone N-methylated. The omphalotin biosynthetic gene cluster codes for the precursor protein OphMA, the protease prolyloligopeptidase OphP and other proteins that are likely to be involved in other post-translational modifications of the peptide. Mining of available fungal genome sequences revealed the existence of highly homologous gene clusters in the basidiomycetes Lentinula edodes and Dendrothele bispora. The respective borosins, referred to as lentinulins and dendrothelins are naturally produced by L. edodes and D. bispora as shown by analysis of respective mycelial extracts. We produced all three homologous peptide natural products by coexpression of OphMA hybrid proteins and OphP in the yeast Pichia pastoris. The recombinant peptides differ in their nematotoxic activity against the plant pathogen Meloidogyne incognita. Our findings pave the way for the production of borosin peptide natural products and their potential application as novel biopharmaceuticals and biopesticides.

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Integrative analysis of chloroplast DNA methylation in a marine alga—Saccharina japonica

Plant Molecular Biology ◽

10.1007/s11103-020-01113-9 ◽

2021 ◽

Author(s):

Linhong Teng ◽

Wentao Han ◽

Xiao Fan ◽

Xiaowen Zhang ◽

Dong Xu ◽

...

Keyword(s):

Dna Methylation ◽

Chloroplast Dna ◽

Marine Alga ◽

Saccharina Japonica ◽

Integrative Analysis

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Neuropeptide Y-based recombinant peptides ameliorate bone loss in mice by regulating hematopoietic stem/progenitor cell mobilization

BMB Reports ◽

10.5483/bmbrep.2017.50.3.191 ◽

2017 ◽

Vol 50 (3) ◽

pp. 138-143 ◽

Cited By ~ 3

Author(s):

Min Hee Park ◽

Namoh Kim ◽

Hee Kyung Jin ◽

Jae-sung Bae

Keyword(s):

Bone Loss ◽

Neuropeptide Y ◽

Progenitor Cell ◽

Hematopoietic Stem ◽

Recombinant Peptides ◽

Cell Mobilization

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Cold Steeping Infusion, a Novel Lectin Extraction Technique for the Isolation, Purification and Partial Characterization of Lectins from the Green Venezuelan Marine Alga Caulerpa serrulata

Natural Product Communications ◽

10.1177/1934578x1801301233 ◽

2018 ◽

Vol 13 (12) ◽

pp. 1934578X1801301

Author(s):

Pablo Djabayan-Djibeyan ◽

Brian Carpenter ◽

Gerardo Medina-Ramírez ◽

Felix Andueza-Leal ◽

Andrés León-Leal ◽

...

Keyword(s):

Molecular Weight ◽

Red Blood Cells ◽

Ammonium Sulfate ◽

Bioactive Compounds ◽

Blood Cells ◽

Marine Alga ◽

Continuous Production ◽

Isotonic Saline ◽

Size Exclusion ◽

Extraction Technique

A lectin from the green Venezuelan marine alga Caulerpa serrulata was extracted with phosphate buffered saline (PBS) using cold steeping infusion (CSI) and by grinding with liquid nitrogen (GLN). The proteins were precipitated using solid ammonium sulfate. Both the crude extracts and ammonium sulfate precipitated proteins were tested for hemagglutinins using native and papain-treated human red blood cell suspensions in isotonic saline solution. Purification of lectins was achieved using affinity chromatography-sugar-epoxy-sepharose 6B and molecular weight was assessed by size exclusion chromatography using Bio-gel® P-100 and SDS-PAGE with 2-mercaptoethanol. IEF-urea 8M was also evaluated. Using CSI it was shown that the marine alga released hemagglutinating compounds into the solutions; the same hemagglutinating compounds were also obtained by GLN. Ammonium sulfate precipitated proteins exhibited agglutinating activity against native and papain-treated human red blood cells. Temperature and EDTA were shown to affect dramatically the lectin activity towards red blood cells. A lectin was purified efficiently and the molecular weight calculated as approximately 78,000 Daltons. The CSI technique demonstrated that the alga could be returned to an active metabolic state by immersion in a simple buffer after having been kept dormant by freezing at −20°C for long periods. It was also shown that the alga was releasing bioactive compounds into the solutions and, therefore, this procedure is being suggested as a good, gentle, non-disruptive extraction technique and we postulate CSI as a possible bioreactor for the continuous production of bioactive compounds from green marine algae.

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