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The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus

tetano

Editor, Senior Moderator
PLoS One. 2016 Jun 6;11(6):e0156929. doi: 10.1371/journal.pone.0156929. eCollection 2016.
[h=1]The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus.[/h] Pinkenburg O[SUP]1[/SUP], Meyer T[SUP]1[/SUP], Bannert N[SUP]2[/SUP], Norley S[SUP]2[/SUP], Bolte K[SUP]3[/SUP], Czudai-Matwich V[SUP]4[/SUP], Herold S[SUP]5[/SUP], Gessner A[SUP]6[/SUP], Schnare M[SUP]1[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] In addition to their well-known antibacterial activity some antimicrobial peptides and proteins (AMPs) display also antiviral effects. A 27 aa peptide from the N-terminal part of human bactericidal/permeability-increasing protein (BPI) previously shown to harbour antibacterial activity inhibits the infectivity of multiple Influenza A virus strains (H1N1, H3N2 and H5N1) the causing agent of the Influenza pneumonia. In contrast, the homologous murine BPI-peptide did not show activity against Influenza A virus. In addition human BPI-peptide inhibits the activation of immune cells mediated by Influenza A virus. By changing the human BPI-peptide to the sequence of the mouse homologous peptide the antiviral activity was completely abolished. Furthermore, the human BPI-peptide also inhibited the pathogenicity of the Vesicular Stomatitis Virus but failed to interfere with HIV and measles virus. Electron microscopy indicate that the human BPI-peptide interferes with the virus envelope and at high concentrations was able to destroy the particles completely.


PMID: 27273104 [PubMed - in process] Free full text
 
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