Universidad Complutense de Madrid
E-Prints Complutense

One single salt bridge explains the different cytolytic activities shown by actinoporins sticholysin I and II from the venom of Stichodactyla helianthus

Impacto

Downloads

Downloads per month over past year



Rivera de Torre, Esperanza and Palacios Ortega, Juan and García Linares, Sara and Gavilanes, José G. and Martínez del Pozo, Álvaro (2017) One single salt bridge explains the different cytolytic activities shown by actinoporins sticholysin I and II from the venom of Stichodactyla helianthus. Archives of Biochemistry and Biophysics, 636 . pp. 79-89.

[img] PDF
Restringido a Repository staff only

1MB

Official URL: http://www.sciencedirect.com/science/article/pii/S000398611730632X?via%3Dihub



Abstract

Sticholysins I and II (StnI and StnII), α-pore forming toxins from the sea anemone Stichodactyla helianthus, are water-soluble toxic proteins which upon interaction with lipid membranes of specific composition bind to the bilayer, extend and insert their N-terminal α-helix, and become oligomeric integral membrane structures. The result is a pore that leads to cell death by osmotic shock. StnI and StnII show 93% of sequence identity, but also different membrane pore-forming activities. The hydrophobicity profile along the first 18 residues revealed differences which were canceled by substituting StnI amino acids 2 and 9. Accordingly, the StnID9A mutant, and the corresponding StnIE2AD9A variant, showed enhanced hemolytic activity. They also revealed a key role for an exposed salt bridge between Asp9 and Lys68. This interaction is not possible in StnII but appears conserved in the other two well-characterized actinoporins, equinatoxin II and fragaceatoxin C. The StnII mutant A8D showed that this single replacement was enough to transform StnII into a version with impaired pore-forming activity. Overall, the results show the key importance of this salt bridge linking the N-terminal stretch to the β-sandwich core. A conclusion of general application for the understanding of salt bridges role in protein design, folding and stability.


Item Type:Article
Uncontrolled Keywords:Pore-forming-toxin; Equinatoxin; Fragaceatoxin; Oligomerization; Ion-channel
Subjects:Sciences > Chemistry > Biochemistry
ID Code:45632
Deposited On:30 Nov 2017 13:53
Last Modified:11 Dec 2017 15:11

Origin of downloads

Repository Staff Only: item control page