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Review
. 2021 Jan 4;19(1):17.
doi: 10.3390/md19010017.

Current Knowledge on Microviridin from Cyanobacteria

Affiliations
Review

Current Knowledge on Microviridin from Cyanobacteria

Samuel Cavalcante do Amaral et al. Mar Drugs. .

Abstract

Cyanobacteria are a rich source of secondary metabolites with a vast biotechnological potential. These compounds have intrigued the scientific community due their uniqueness and diversity, which is guaranteed by a rich enzymatic apparatus. The ribosomally synthesized and post-translationally modified peptides (RiPPs) are among the most promising metabolite groups derived from cyanobacteria. They are interested in numerous biological and ecological processes, many of which are entirely unknown. Microviridins are among the most recognized class of ribosomal peptides formed by cyanobacteria. These oligopeptides are potent inhibitors of protease; thus, they can be used for drug development and the control of mosquitoes. They also play a key ecological role in the defense of cyanobacteria against microcrustaceans. The purpose of this review is to systematically identify the key characteristics of microviridins, including its chemical structure and biosynthesis, as well as its biotechnological and ecological significance.

Keywords: biotechnology; cyanobacteria; ecology; microviridin; oligopeptide.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Diversity of microviridin sequences and the conserved KYPSD motif. Multiple alignment was obtained by Clustal Omega (https://www.ebi.ac.uk) and visualized using JalView software (https://www.jalview.org), and the consensus sequence was generated by WebLogo (https://weblogo.berkeley.edu).
Figure 2
Figure 2
Microviridin structures belonging to group I.
Figure 2
Figure 2
Microviridin structures belonging to group I.
Figure 3
Figure 3
Microviridin structures belonging to group II.
Figure 4
Figure 4
Microviridin structure belonging to group III.
Figure 5
Figure 5
Microviridin structure belonging to group IV.
Figure 6
Figure 6
Graphical representation of microviridin biosynthetic clusters. The gene cluster compilation was accomplished through the Gene Graphics application (https://katlabs.cc/genegraphics/app).
Figure 7
Figure 7
Leader peptide sequences from different microviridins. The PFFARFL motif is highly conversed among them. This sequence and some of its flanking amino acids are structured as an α-helix, responsible for recognition by ATP-grasp ligases. Multiple alignment was obtained by Clustal Omega (https://www.ebi.ac.uk) and visualized using JalView software (https://www.jalview.org).
Figure 8
Figure 8
Microviridin biosynthesis. (A) Ester bond formations by MvdD/MdnC. (B) Amide bond formations by MvdC/MdnB. (C) Removal of a peptide leader by a proteolytic enzyme. (D) N-acetylation by MvdB/MdnD.
Figure 9
Figure 9
Ecological role of microviridins as antifeedant against the microcrustacean Daphnia.
Figure 10
Figure 10
Potential applications of microviridins.
Figure 11
Figure 11
Interaction between microviridin J and trypsin at pH 8.5 (Protein Data Bank (PDB) code: 4KTS). (A) 3D representation of the interaction. (B) 2D view of the major interaction between microviridin J and trypsin. Hydrogen bonds are in green, while the hydrophobic interactions are in red.

References

    1. Kulasooriya S. Cyanobacteria: Pioneers of Planet Earth. Ceylon J. Sci. 2012;40:71.
    1. Vijay D., Akhtar M., Hess W. Genetic and metabolic advances in the engineering of cyanobacteria. Curr. Opin. Biotechnol. 2019;59:150–156. - PubMed
    1. Singh P.K., Rai S., Pandey S., Agrawal C., Shrivastava A.K., Kumar S., Rai L.C. Cadmium and UV-B induced changes in proteome and some biochemical attributes of Anabaena sp. PCC7120. Phykos. 2012;42:39–50.
    1. Koch R., Kupczok A., Stucken K., Ilhan J., Hammerschmidt K., Dagan T. Plasticity first: Molecular signatures of a complex morphological trait in filamentous cyanobacteria. BMC Evol. Biol. 2017;17:1–11. - PMC - PubMed
    1. Abed R., Dobretsov S., Sudesh K. Applications of cyanobacteria in biotechnology. J. Appl. Microbiol. 2009;106:1–12. - PubMed

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