A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells

Avian influenza viruses (AIV), the causative agent of avian flu or bird flu, cause widespread morbidity and mortality in poultry. The symptoms of the disease range from mild flu like symptoms to death. These viruses possess two important surface glycoproteins, namely hemagglutinin (HA) and neuramini...

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Main Authors: Rajik, Mohamed, Omar, Abdul Rahman, Ideris, Aini, Hassan, Sharifah Syed, Yusoff, Khatijah
Format: Text
Language:English
Published: Ivyspring International Publisher 2009
Subjects:
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2726580
http://www.ncbi.nlm.nih.gov/pubmed/19680476
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spelling ftpubmed:oai:pubmedcentral.nih.gov:2726580 2023-05-15T15:34:27+02:00 A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells Rajik, Mohamed Omar, Abdul Rahman Ideris, Aini Hassan, Sharifah Syed Yusoff, Khatijah 2009-08-08 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2726580 http://www.ncbi.nlm.nih.gov/pubmed/19680476 en eng Ivyspring International Publisher http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2726580 http://www.ncbi.nlm.nih.gov/pubmed/19680476 © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited. CC-BY-NC-ND Short Research Communication Text 2009 ftpubmed 2013-09-02T15:43:39Z Avian influenza viruses (AIV), the causative agent of avian flu or bird flu, cause widespread morbidity and mortality in poultry. The symptoms of the disease range from mild flu like symptoms to death. These viruses possess two important surface glycoproteins, namely hemagglutinin (HA) and neuraminidase (NA) against which neutralizing antibodies are produced. Due to the highly mutative nature of the genes which encode these proteins, the viruses often confer resistance to the current anti-viral drugs making the prevention and treatment of infection challenging. In our laboratory, we have recently identified a novel anti-viral peptide (P1) against the AIV H9N2 from a phage displayed peptide library. This peptide inhibits the replication of the virus in ovo and in vitro by its binding to the HA glycoprotein. In the current study, we demonstrate that the peptide inhibits the virus replication by preventing the attachment to the host cell but it does not have any effect on the viral fusion. The reduction in the viral nucleoprotein (NP) expression inside the host cell has also been observed during the peptide (P1) treatment. This novel peptide may have the potential to be developed as a therapeutic agent for the treatment and control of avian influenza virus H9N2 infections. Text Avian flu PubMed Central (PMC)
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Short Research Communication
spellingShingle Short Research Communication
Rajik, Mohamed
Omar, Abdul Rahman
Ideris, Aini
Hassan, Sharifah Syed
Yusoff, Khatijah
A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells
topic_facet Short Research Communication
description Avian influenza viruses (AIV), the causative agent of avian flu or bird flu, cause widespread morbidity and mortality in poultry. The symptoms of the disease range from mild flu like symptoms to death. These viruses possess two important surface glycoproteins, namely hemagglutinin (HA) and neuraminidase (NA) against which neutralizing antibodies are produced. Due to the highly mutative nature of the genes which encode these proteins, the viruses often confer resistance to the current anti-viral drugs making the prevention and treatment of infection challenging. In our laboratory, we have recently identified a novel anti-viral peptide (P1) against the AIV H9N2 from a phage displayed peptide library. This peptide inhibits the replication of the virus in ovo and in vitro by its binding to the HA glycoprotein. In the current study, we demonstrate that the peptide inhibits the virus replication by preventing the attachment to the host cell but it does not have any effect on the viral fusion. The reduction in the viral nucleoprotein (NP) expression inside the host cell has also been observed during the peptide (P1) treatment. This novel peptide may have the potential to be developed as a therapeutic agent for the treatment and control of avian influenza virus H9N2 infections.
format Text
author Rajik, Mohamed
Omar, Abdul Rahman
Ideris, Aini
Hassan, Sharifah Syed
Yusoff, Khatijah
author_facet Rajik, Mohamed
Omar, Abdul Rahman
Ideris, Aini
Hassan, Sharifah Syed
Yusoff, Khatijah
author_sort Rajik, Mohamed
title A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells
title_short A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells
title_full A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells
title_fullStr A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells
title_full_unstemmed A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells
title_sort novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells
publisher Ivyspring International Publisher
publishDate 2009
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2726580
http://www.ncbi.nlm.nih.gov/pubmed/19680476
genre Avian flu
genre_facet Avian flu
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2726580
http://www.ncbi.nlm.nih.gov/pubmed/19680476
op_rights © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.
op_rightsnorm CC-BY-NC-ND
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