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. 2019 Apr 8;17(4):216.
doi: 10.3390/md17040216.

Soritesidine, a Novel Proteinous Toxin from the Okinawan Marine Sponge Spongosorites sp

Ryuichi Sakai  1 , Kota Tanano  2 , Takumi Ono  3 , Masaya Kitano  4 , Yusuke Iida  5 , Koji Nakano  6 , Mitsuru Jimbo  7
Affiliations

Soritesidine, a Novel Proteinous Toxin from the Okinawan Marine Sponge Spongosorites sp

Ryuichi Sakai et al. Mar Drugs. .

Abstract

A novel protein, soritesidine (SOR) with potent toxicity was isolated from the marine sponge Spongosorites sp. SOR exhibited wide range of toxicities over various organisms and cells including brine shrimp (Artemia salina) larvae, sea hare (Aplysia kurodai) eggs, mice, and cultured mammalian cells. Toxicities of SOR were extraordinary potent. It killed mice at 5 ng/mouse after intracerebroventricular (i.c.v.) injection, and brine shrimp and at 0.34 µg/mL. Cytotoxicity for cultured mammalian cancer cell lines against HeLa and L1210 cells were determined to be 0.062 and 12.11 ng/mL, respectively. The SOR-containing fraction cleaved plasmid DNA in a metal ion dependent manner showing genotoxicity of SOR. Purified SOR exhibited molecular weight of 108.7 kDa in MALDI-TOF MS data and isoelectric point of approximately 4.5. N-terminal amino acid sequence up to the 25th residue was determined by Edman degradation. Internal amino acid sequences for fifteen peptides isolated from the enzyme digest of SOR were also determined. None of those amino acid sequences showed similarity to existing proteins, suggesting that SOR is a new proteinous toxin.

Keywords: brine shrimp; cytotoxicity; genotoxin; mouse lethality; protein; sponge.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
(A) Brine shrimp lethality of the crude extract after heat treatments, (B) ultrafiltration fraction using 30 kDa membrane, (C) treated in different buffers with various pH. All animals survived in both control and the filtrate groups.
Figure 2
Figure 2
(A) An elution of the active soritesidine (SOR) in a size exclusion chromatography (Superdex 200–300). (B) SDS-PAGE for Fraction A; M, size marker, 1, Fraction A.
Figure 3
Figure 3
(a) Purification scheme of SOR, and (b) SDS-PAGE at each step; M, size marker; 1, AS-80; 2, active fraction-HP; 3, active fraction-AE; 4, soritesidine.
Figure 4
Figure 4
(a) A MALDI-TOF mass data for SOR, and (b) a two dimensional gel electrophoresis of AS-80. An arrow indicates a spot for SOR.
Figure 5
Figure 5
Concentration dependent inhibition by SOR; (a) against mouse lymphoma cell line L1210 and human tumor cell line HeLa, (b) against brine shrimp larvae at three different observation periods.
Figure 6
Figure 6
Sea hare eggs 6 h (a) and 24 h (b) after fertilization. Those treated with SOR (1.3 µg/mL, c,d), and with 1.3 ng/mL (e,f). An arrow indicates a bubble-like protrusion on the surface of egg.
Figure 7
Figure 7
A mouse received SOR via i.c.v. Mouse losing activity 14 h after administration. (a) Red ring around eyes started to build up. (b) Red ring became conspicuous after 16 h.
Figure 8
Figure 8
Cleavage of plasmid DNA upon treatment by SOR; line 1, size marker, 2, plasmid DNA, 3, plasmid DNA + SOR, 4, plasmid DNA + SOR + EDTA, a band with lower mobility is a nicked plasmid.
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References

    1. Fusetani N., Matsunaga S. Bioactive sponge peptides. Chem. Rev. 1993;93:1793–1806. doi: 10.1021/cr00021a007. - DOI
    1. Gogineni V., Hamann M.T. Marine natural product peptides with therapeutic potential: Chemistry, biosynthesis, and pharmacology. Biochim. Biophys. Acta. 2018;1862:81–196. doi: 10.1016/j.bbagen.2017.08.014. - DOI - PMC - PubMed
    1. Hamada T., Matsunaga S., Yano G., Fusetani N. Polytheonamides a and b, highly cytotoxic, linear polypeptides with unprecedented structural features, from the marine sponge, Theonella swinhoei. J. Am. Chem. Soc. 2005;127:110–118. doi: 10.1021/ja045749e. - DOI - PubMed
    1. Takada K., Hamada T., Hirota H., Nakao Y., Matsunaga S., van Soest R.W., Fusetani N. Asteropine a, a sialidase-inhibiting conotoxin-like peptide from the marine sponge Asteropus simplex. Chem. Biol. 2006;13:569–574. doi: 10.1016/j.chembiol.2006.05.010. - DOI - PubMed
    1. Li H., Bowling J.J., Fronczek F.R., Hong J., Jabba S.V., Murray T.F., Ha N.-C., Hamann M.T., Jung J.H. Asteropsin a: An unusual cystine-crosslinked peptide from porifera enhances neuronal Ca2+ influx. Biochim. Biophys. Acta. 2013;1830:2591–2599. doi: 10.1016/j.bbagen.2012.11.015. - DOI - PMC - PubMed

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