Native Herpes Simplex Virus type 1 (HSV type 1) protease has a rather low activity. It has been found however, that the presence of a kosmotropic anion can increase the activity of the protease over 10-fold. This has many advantages, as now assays for protease activity may be run in very small (micromolar and less) amounts of reagents and substrates, and the assays can be run quickly. Activate HSV-1 protease represents a conformational change from native protease.

Merck &amp; Co., Inc.

Activation of herpes simplex virus protease by kosmotropes

A method of purifying proteases from the Herpes Simplex Virus 1 and 2 is taught. A precursor protease is cloned in a host cell and then separated from the cell culture using cation exchange chromatography. The resulting protease is subjected to autoprocessing conditions and an autolytic cleavage occurs, resulting in mature protease.

Purified herpes simplex virus protease and methods of purification

Infectious human cytomegalovirus (HCMV) were isolated in vitro from a pool of randomized sequences after sixteen or 21 cycles of selection and amplification. The ligands characterized exhibited high HCMV-binding affinity in vitro and effectively inhibited viral infection in tissue culture. Several ligands blocked viral entry. Their antiviral activity was also specific as the ligands only reacted with strains of HCMV, but not with the related herpes simplex virus 1 and human cells. Moreover, the ligands recognize several different epitopes. Thus, RNA ligands can function to bind to a human virus and block viral infection. The screening method may utilize the novel features of binding to intact infectious virus, partitioning the bound polynucleotides from unbound by passing through a porous filter, and enhancing the release of bound polynucleotides by treatment with protease.

herpes simplex/protease

Activation of herpes simplex virus protease by kosmotropes

Purified herpes simplex virus protease and methods of purification

Polynucleotide ligands as anti-viral agents

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