Direct inactivation of viruses by XXXX granulocyte defensins.

@entity1 @entity778 @entity20622 @entity8310 @entity5765 @entity38675 @entity3307
@entity1 neutrophils contain a family of microbicidal peptides known as defensins. One of these defensins, @entity1 @entity38675 , was purified, and its ability to directly inactivate several viruses was extensively tested. @entity778 and 2, @entity8310 virus, and influenza virus A/ @entity20622 were inactivated by incubation with @entity38675 . Two nonenveloped viruses, echovirus type 11 and @entity5765 , were resistant to inactivation. Purified homologous peptides @entity778 and HNP-3 were found to have @entity3307 -neutralizing activities approximately equal to that of @entity38675 . Inactivation of @entity3307 by @entity38675 depended on the time, temperature, and pH of incubation. Antiviral activity was abrogated by low temperature or prior reduction and alkylation of the defensins. Addition of serum or serum albumin to the incubation mixtures inhibited neutralization of @entity3307 by @entity38675 . We used density gradient sedimentation techniques to demonstrate that @entity38675 bound to @entity3307 in a temperature-dependent manner. We speculate that binding of defensin peptides to certain viruses may impair their ability to infect cells.
