Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita

Шенкарев, Захар О.; Panteleev, Pavel V.; Balandin, Sergey V.; Gizatullina, Albina K.; Altukhov, Dmitry A.; Finkina, Ekaterina I.; Kokryakov, V. N.; Arseniev, Alexander S.; Ovchinnikova, Tatiana V.

doi:10.1016/j.bbrc.2012.10.092

Cited by 47 publications

(20 citation statements)

References 26 publications

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“…18) and a number of neurotoxins of spiders [55,56], and aurelin from a mesoglea of the Aurelia aurita scyphozoan jellyfish (no. 4) and the BgK and ShK blockers of potassium channels from the venom of sea anemones [37] (Fig. 1).…”

Section: Cysteine Containing Amps Which Are Stabilizedmentioning

confidence: 99%

Antimicrobial peptides of invertebrates. Part 1. structure, biosynthesis, and evolution

Balandin

Ovchinnikova

2016

Russ J Bioorg Chem

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Antimicrobial peptides and proteins (AMPs) are among the most important components of the immune system of multicellular organisms. The role of AMPs is of particular importance for invertebrates which constitute the vast majority of species diversity of the living world, because these animals lack acquired immunity. The AMPs of animal origin are ribosomally synthesized molecules that have, as a rule, a positive net charge and amphiphilic properties. They can act against bacteria, yeast and filamentous fungi, protozoa, and enveloped viruses. AMPs can also play a role of mediators of the immune system. Search and investiga tion for protective factors of the invertebrate host defense provide a better understanding of mechanisms of the innate immunity of humans and other mammals and give a key to a development of new medicines. The first part of this review focuses on special features of a structure, biosynthesis, regulation of gene expression, and molecular evolution of AMPs of invertebrates.

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Section: Cysteine Containing Amps Which Are Stabilizedmentioning

confidence: 99%

Antimicrobial peptides of invertebrates. Part 1. structure, biosynthesis, and evolution

Balandin

Ovchinnikova

2016

Russ J Bioorg Chem

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“…Defensin-like AMPs with cysteine connectivity (C1-C6, C2-C4, and C3-C5) identified thus far from cnidarian species (e.g., aurelin and damicornin) share a common ancestor and key structural features, including CSab motifs, with invertebrate defensins exhibiting cysteine connectivity (C1-C4, C2-C5, and C3-C6) ( Fig. 5B) [20,40]. In contrast, Crassicorin-I exhibits cysteine arrangement differing from that of cnidarian defensin-like AMPs.…”

Section: Crassicorin-i Is Generated From a Large Precursor Preprocramentioning

confidence: 99%

Defensin‐neurotoxin dyad in a basally branching metazoan sea anemone

Kim

Lee

et al. 2017

The FEBS Journal

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Recent studies suggest that vertebrate and invertebrate defensins have evolved from two independent ancestors, and that both defensins could share origins with animal toxins. Here, we purified novel sea anemone neurotoxin (BDS)-like antimicrobial peptides (AMPs)-Crassicorin-I and its putative homolog (Crassicorin-II)-from the pharynx extract of an anthozoan sea anemone (Urticina crassicornis). Based on structural analyses and cDNA cloning, mature Crassicorin-I represents a cationic AMP likely generated from a precursor and comprising 40 amino acid residues, including six cysteines forming three intramolecular disulfide bonds. Recombinant Crassicorin-I produced in a heterologous bacterial-expression system displayed antimicrobial activity against both a gram-positive bacterium (Bacillus subtilis) and gram-negative bacteria (Escherichia coli and Salmonella enterica). The Crassicorin-I transcript was upregulated by immune challenge, suggesting its involvement in defense mechanisms against infectious pathogens in sea anemone. Sequence alignment and three-dimensional molecular modeling revealed that Crassicorin-I exhibits high degrees of structural similarity to sea anemone neurotoxins that share β-defensin fold which is found in vertebrate defensins and invertebrate big-defensins. Consistent with its structural similarity to neurotoxins, Crassicorin-I exhibited paralytic activity toward a crustacean. These findings motivated our investigation and subsequent discovery of antimicrobial activity from other known sea anemone neurotoxins, such as APETx1 and ShK. Collectively, our work signified that Crassicorin-I is the first AMP identified from a sea anemone and provided evidence of a functional linkage between AMPs and neurotoxins in a basally branching metazoan.

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“…For instance, hydralysin is a noncnidocystic neurotoxin from the hydra Chlorohydra viridissima (Zhang et al, 2003). Likewise, the antimicrobial peptide aurelin was extracted and characterized from the mesoglea of Aurelia aurita (Ovchinnikova et al, 2006;Shenkarev et al, 2012). Nematocyst-free tentacle extract from Chironex fleckeri had a cardiotoxic effect in anaesthetized rats, which differed from the effect of nematocyst extract (Ramasamy et al, 2005a).…”

Section: Venom Localizationmentioning

confidence: 99%

Bioactive toxins from stinging jellyfish

Badré

2014

Toxicon

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Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita

Cited by 47 publications

References 26 publications

Antimicrobial peptides of invertebrates. Part 1. structure, biosynthesis, and evolution

Antimicrobial peptides of invertebrates. Part 1. structure, biosynthesis, and evolution

Defensin‐neurotoxin dyad in a basally branching metazoan sea anemone

Bioactive toxins from stinging jellyfish

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