Adeno-Associated virus 8 delivers an immunomodulatory peptide to mouse liver more efficiently than to rat liver. [PDF]
Targeting the Kv1.3 potassium channel has proven effective in reducing obesity and the severity of animal models of autoimmune disease. Stichodactyla toxin (ShK), isolated from the sea anemone Stichodactyla helianthus, is a potent blocker of Kv1.3 ...
Yuqing Wang +7 more
doaj +7 more sources
Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea Anemone Stichodactyla helianthus. [PDF]
Venoms constitute complex mixtures of many different molecules arising from evolution in processes driven by continuous prey–predator interactions. One of the most common compounds in these venomous cocktails are pore-forming proteins, a family of toxins whose activity relies on the disruption of the plasmatic membranes by forming pores.
Rivera-de-Torre E +5 more
europepmc +10 more sources
Stichodactyla helianthus' de novo transcriptome assembly: Discovery of a new actinoporin isoform [PDF]
Transcriptomic profiling of venom producing tissues from different animals is an effective approach for discovering new toxins useful in biotechnological and pharmaceutical applications, as well in evolutionary comparative studies of venomous animals ...
Garb, Jessica E. +2 more
core +9 more sources
Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus. [PDF]
The BPTI/Kunitz-type inhibitor family includes several extremely potent serine protease inhibitors. To date, the inhibitory mechanisms have only been studied for mammalian inhibitors. Here, the first crystal structure of a BPTI/Kunitz-type inhibitor from a marine invertebrate (rShPI-1A) is reported to 2.5 Å resolution.
García-Fernández R +8 more
europepmc +7 more sources
Effects of lipid composition on membrane permeabilization by sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus. [PDF]
Sticholysin I and II (St I and St II), two basic cytolysins purified from the Caribbean sea anemone Stichodactyla helianthus, efficiently permeabilize lipid vesicles by forming pores in their membranes. A general characteristic of these toxins is their preference for membranes containing sphingomyelin (SM).
Valcarcel CA +8 more
europepmc +6 more sources
The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface [PDF]
Actinoporins are α-pore forming proteins with therapeutic potential, produced by sea anemones. Sticholysin II (StnII) from Stichodactyla helianthus is one of its most extensively characterized members.
Sara García-Linares +5 more
doaj +7 more sources
The Mitochondrial Genome of the Sea Anemone Stichodactyla haddoni Reveals Catalytic Introns, Insertion-Like Element, and Unexpected Phylogeny. [PDF]
A hallmark of sea anemone mitochondrial genomes (mitogenomes) is the presence of complex catalytic group I introns. Here, we report the complete mitogenome and corresponding transcriptome of the carpet sea anemone Stichodactyla haddoni (family ...
Johansen SD +3 more
europepmc +4 more sources
Screening and cDNA Cloning of Kv1 Potassium Channel Toxins in Sea Anemones [PDF]
When 21 species of sea anemones were screened for Kv1 potassium channel toxins by competitive inhibition of the binding of 125I-α-dendrotoxin to rat synaptosomal membranes, 11 species (two species of Actiniidae, one species of Hormathiidae, five species ...
Kazuo Shiomi +4 more
doaj +4 more sources
Genomic, functional and structural analyses elucidate evolutionary innovation within the sea anemone 8 toxin family [PDF]
Background The ShK toxin from Stichodactyla helianthus has established the therapeutic potential of sea anemone venom peptides, but many lineage-specific toxin families in Actiniarians remain uncharacterised. One such peptide family, sea anemone 8 (SA8),
Lauren M. Ashwood +22 more
doaj +2 more sources
N-Terminally extended analogues of the K⁺ channel toxin from Stichodactyla helianthus as potent and selective blockers of the voltage-gated potassium channel Kv1.3. [PDF]
Chang SC +6 more
europepmc +3 more sources

