Evaluation of the Inactivation of Infectious Herpes Simplex Virus by Host-Defense Peptides
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A 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide microplate assay was adapted to screen for the ability of 20 host-defense peptides to inactivate herpes simplex virus type 1 and type 2. The procedure required minimal amounts of material, was reproducible, and was confirmed with standard antiviral testing techniques. In screening tests, with the exception of melittin, a highly cytotoxic and hemolytic peptide found in bee venom, the α-helical peptides in our test panel (magainins, cecropins, clavanins, and LL-37) caused little viral inactivation. Several β-sheet peptides (defensins, tachyplesin, and protegrins) inactivated one or both viruses, sometimes with remarkable selectivity. Two peptides were identified as having antiviral activity against both viruses, indolicidin (a tryptophan-rich peptide from bovine neutrophils) and brevinin-1 (a peptide found in frog skin). The antiviral activity of these two peptides was confirmed with standard antiviral assays. Interestingly, the antiviral activity of brevinin-1 was maintained after reduction and carboxamidomethylation, procedures that abolished its otherwise prominent hemolytic and cytotoxic effects.
- Evaluation of the Inactivation of Infectious Herpes Simplex Virus by Host-Defense Peptides
European Journal of Clinical Microbiology and Infectious Diseases
Volume 19, Issue 3 , pp 187-194
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- A1. Department of Pathology and Laboratory Medicine, UCLA School of Medicine, CHS 1P-244, Los Angeles, CA 90095–1731, USA e-mail: email@example.com, US
- A2. Department of Medicine, UCLA School of Medicine, CHS 37–062, Los Angeles, CA 90095–1690, USA, US