tetano
Editor, Senior Moderator
J Gen Virol. 2012 Jan 18. [Epub ahead of print]
A novel family of peptides with potent activity against influenza A viruses.
Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA.
Source
University of Edinburgh.
Abstract
The emergence of drug resistant strains of influenza virus has catalyzed a search for new antiviral agents to supplement or replace existing drugs. Following the success of the HIV entry blocker Enfuvirtide, there has been a resurgence of interest in peptide based antivirals. In this paper we report on the discovery of a novel family of peptides (FluPep, FP) that function as inhibitors of influenza A virus infection. The prototype peptide (FP1, also known as Tkip) interacts with haemagglutinin and inhibits the binding of the virus to cell membranes. Using a plaque reduction assay we have demonstrated that a variety of influenza A virus subtypes (including H1N1, H3N2 H5N1) are inhibited by FluPep and its derivatives at nanomolar concentrations. By truncating FluPep we have identified a minimal sequence of 6 amino acids that binds to HA and inhibits infection. Using a mouse model of intranasal influenza virus infection we observed potent inhibition of virus infection when peptide is given at the time of virus administration. These data indicate that FluPep is a highly effective anti-influenza agent with the potential to translate to the clinic.
PMID:
22258859
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22258859
A novel family of peptides with potent activity against influenza A viruses.
Nicol MQ, Ligertwood Y, Bacon MN, Dutia BM, Nash AA.
Source
University of Edinburgh.
Abstract
The emergence of drug resistant strains of influenza virus has catalyzed a search for new antiviral agents to supplement or replace existing drugs. Following the success of the HIV entry blocker Enfuvirtide, there has been a resurgence of interest in peptide based antivirals. In this paper we report on the discovery of a novel family of peptides (FluPep, FP) that function as inhibitors of influenza A virus infection. The prototype peptide (FP1, also known as Tkip) interacts with haemagglutinin and inhibits the binding of the virus to cell membranes. Using a plaque reduction assay we have demonstrated that a variety of influenza A virus subtypes (including H1N1, H3N2 H5N1) are inhibited by FluPep and its derivatives at nanomolar concentrations. By truncating FluPep we have identified a minimal sequence of 6 amino acids that binds to HA and inhibits infection. Using a mouse model of intranasal influenza virus infection we observed potent inhibition of virus infection when peptide is given at the time of virus administration. These data indicate that FluPep is a highly effective anti-influenza agent with the potential to translate to the clinic.
PMID:
22258859
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22258859