A novel role for 3-O(ital)-sulfated heparan sulfate in herpes simplex virus 1 entry

Article Abstract:

A novel role for 3-O(ital)-sulfated heparan sulfate (HS) found in herpes simplex virus 1 (HSV-1) entry is discussed. HSV-1 binds to cells by interactions of viral glycoproteins gB and gC with HS chains on proteoglycans on the cell surface. The binding is not sufficient for viral entry. Fusion between viral envelope and cell membrane is necessary. It has been shown that heparan sulfate modified by a subset of the multiple D-glucosaminyl 3-O(ital)-sulfotransferase isoforms furnishes sites for the binding of a third viral glycoprotein, gD, and for starting HSV-1 entry. Susceptibility of cells to HSF-1 entry depends on two factors.

Viruses, Herpes simplex virus

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The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins

Article Abstract:

Membrane insertion for a cholesterol-dependent cytolysin (CDC) is discussed relative to its mechanism. Existence of a region in domain 3 of perfringolysin O (PFO) that interacts with the membrane and undergoes an alpha-helical to beta-strand transition is described. PFO is a water-soluble monomeric cytolysin secreted by Clostridium perfringens. Insertion of two transmembrane hairpins per toxin monomer and the great change in secondary structure are remarkable. They make up a novel paradigm for the mechanism of membrane insertion by a cytolytic toxin.

Australia, Genetic aspects, Clostridium, Cholesterol

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HIV-1 entry inhibitors in the side pocket

Article Abstract:

HIV-1 entry inhibitors in the side pocket are discussed in this review article. Topics include the bp41 glycoprotein as a target for intervention and targeting the N36 pocket for drug development. Probably more reduction in size of the D10-pS-2K peptides will be needed to find a clinically usable therapeutic. Researchers likely will have to exploit the potential of nonpeptide molecules to fill the N36 pocket more efficiently than the natural C34 residues.

HIV (Viruses), HIV, Glycoproteins, Viral envelopes

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