Transmembrane pores

Ebook "Proteins: Membrane binding and pore formation" describes how several of the important pore forming toxin families achieve membrane bi- ing and which structural elements are used for formation of transmembrane pores. Our contributors have thus provided the means for a comparative analysis of several unrelated families.

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Alpha-helical transmembrane channel and transporter proteins play vital roles in a diverse range of essential biological processes and are crucial in facilitating the passage of ions and molecules across the lipid bilayer.

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Understanding channel structures that lead to active sites or traverse the molecule is important in the study of molecular functions such as ion, ligand, and small molecule transport. Efficient methods for extracting, storing, and analyzing protein channels are required to support such studies.

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Bacterial toxins have evolved to an effective therapeutic option for cancer therapy. The Clostridium perfringens enterotoxin (CPE) is a pore-forming toxin with selective cytotoxicity. The transmembrane tight junction proteins claudin-3 and -4 are known high affinity CPE receptors. Their expression is highly upregulated in human cancers, including breast, ovarian and colon carcinoma.

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Vibrio choleraehemolysin (HlyA), a water-soluble protein with a native monomeric relative molecular mass of 65 000, forms transmembrane pentameric channels in target bio-membranes.TheHlyAbinds to lipid vesicles nonspecifically and without saturation; however, self-assembly is triggered specifically by cholesterol.Here we show that the HlyA partitioned quantitatively to amphiphilic media irrespective of their compositions, indicating that the toxin had an amphiphilic surface.

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Equinatoxin II is a cytolytic protein isolated from the sea anemoneActi-nia equina. It is a member of the actinoporins, a family of eukaryotic pore-forming toxins with a unique mechanism of pore formation. Equinatoxin II is a 20 kDa cysteineless protein, with sphingomyelin-dependent activity. Recent studies showed that the N-terminal region of the molecule requires conformational flexibility during pore formation.

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The prokaryotic potassium channel fromStreptomyces lividans, KcsA, is the first channel that has a known crystal structure of the transmembrane domain. The crystal structure of its soluble C-terminal domain, however, still remains elusive.

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Semi-intact cells are cells whose plasma membrane has been permeabilized with detergent or toxins, and can be referred to as “cell-type test tubes” (Fig. 1). We use a bacterial poreforming toxin, streptolysin O (SLO), to permeabilize the cells. At 4℃, SLO binds to cholesterol in plasma membranes. At warmer temperatures, SLO assembles to form amphiphilic oligomers, which results in the generation of small, stable transmembrane pores (Bhakdi et al., 1985).

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