e-journal

Inhibition of influenza virus replication by constrained peptides targeting nucleoprotein

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Background: Because of high mutation rates, new drugresistant viruses are rapidly evolving, thus making the
necessary control of influenza virus infection difficult.Methods: We screened a constrained cysteine-rich
peptide library mimicking m-conotoxins from Conus geographus and a proline-rich peptide library mimicking
lebocin 1 and 2 from Bombyx mori by using influenza virus RNA polymerase (PB1, PB2 and PA) and
nucleoprotein (NP) as baits. Results: Among the 22 peptides selected from the libraries,we found that the NP-binding proline-rich peptide,PPWCCCSPMKRASPPPAQSDLPATPKCPP, inhibited influenza replicon activity to mean ±sd 40.7% ±15.8%
when expressed as a GFP fusion peptide in replicon cells.Moreover, when the GFP fusion peptide was transduced
into cells by an HIV-TAT protein transduction domain sequence, the replication of influenza virus A/WSN/33
(WSN) at a multiplicity of infection of 0.01 was inhibited to 20% and 69% at 12 and 24 h post-infection, respectively.
In addition, the TAT-GFP fusion peptide was able to slightly protect Balb/c mice from WSN infection when
administrated prior to the infection. Conclusions: These results suggest the potential of this
peptide as the seed of an anti-influenza drug and reveal the usefulness of the constrained peptide strategy for
generating inhibitors of influenza infection. The results also suggest that influenza NP, which is conserved among the influenza A viruses, is a good target for influenza inhibition, despite being the most abundant protein in
infected cells.

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Informasi Detail

Judul Seri

Antiviral Chemistry & Chemotherapy

No. Panggil

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Penerbit

: International Medical Press., 2011

Deskripsi Fisik

Antiviral Chemistry & Chemotherapy 2011; 22:119–130

Bahasa

English

ISBN/ISSN

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Klasifikasi

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Tipe Isi

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Tipe Media

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Tipe Pembawa

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Edisi

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Subjek

PSIKOLOGI SOSIAL

Info Detail Spesifik

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Pernyataan Tanggungjawab

Wati/Agus

Versi lain/terkait

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