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Comparative Study
. 1996 Mar 5;93(5):2186-91.
doi: 10.1073/pnas.93.5.2186.

Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion

D M Lambert  1 , S Barney, A L Lambert, K Guthrie, R Medinas, D E Davis, T Bucy, J Erickson, G Merutka, S R Petteway Jr
Affiliations
Comparative Study

Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion

D M Lambert et al. Proc Natl Acad Sci U S A. .

Abstract

The synthetic peptides DP-107 and DP-178 (T-20), derived from separate domains within the human immunodeficiency virus type 1 (HIV-1) transmembrane (TM) protein, gp4l, are stable and potent inhibitors of HIV-1 infection and fusion. Using a computer searching strategy (computerized antiviral searching technology, C.A.S.T.) based on the predicted secondary structure of DP-107 and DP-178 (T-20), we have identified conserved heptad repeat domains analogous to the DP-107 and DP-178 regions of HIV-1 gp41 within the glycoproteins of other fusogenic viruses. Here we report on antiviral peptides derived from three representative paramyxoviruses, respiratory syncytial virus (RSV), human parainfluenza virus type 3 (HPIV-3), and measles virus (MV). We screened crude preparations of synthetic 35-residue peptides, scanning the DP-178-like domains, in antiviral assays. Peptide preparations demonstrating antiviral activity were purified and tested for their ability to block syncytium formation. Representative DP-178-like peptides from each paramyxovirus blocked homologous virus-mediated syncytium formation and exhibited EC50 values in the range 0.015-0.250 microM. Moreover, these peptides were highly selective for the virus of origin. Identification of biologically active peptides derived from domains within paramyxovirus F1 proteins analogous to the DP-178 domain of HIV-1 gp4l is compelling evidence for equivalent structural and functional features between retroviral and paramyxoviral fusion proteins. These antiviral peptides provide a novel approach to the development of targeted therapies for paramyxovirus infections.

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References

    1. Virology. 1974 Feb;57(2):475-90 - PubMed
    1. Immunol Rev. 1994 Aug;140:93-104 - PubMed
    1. Int J Pept Protein Res. 1978 Mar;11(3):246-9 - PubMed
    1. Methods Biochem Anal. 1985;31:61-163 - PubMed
    1. Science. 1985 Sep 27;229(4720):1402-5 - PubMed

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