The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus.
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.
Institute for Immunology, Philipps-University of Marburg, Marburg, Germany.
Olaf
O
Pinkenburg
Institute for Immunology, Philipps-University of Marburg, Marburg, Germany.
Torben
T
Meyer
Department for HIV and other Retroviruses, Robert Koch Institute, Berlin, Germany.
Norbert
N
Bannert
Department for HIV and other Retroviruses, Robert Koch Institute, Berlin, Germany.
Steven
S
Norley
Laboratory for Cell Biology, Philipps-University of Marburg, Marburg, Germany.
Kathrin
K
Bolte
Institute for Virology, Philipps-University of Marburg, Marburg, Germany.
Volker
V
Czudai-Matwich
Department of Internal Medicine II, University of Giessen Lung Center and German Center for Lung Research, Giessen, Germany.
Susanne
S
Herold
Institute for Clinical Microbiology and Hygiene, University Regensburg, Regensburg, Germany.
André
A
Gessner
Institute for Immunology, Philipps-University of Marburg, Marburg, Germany.
Markus
M
Schnare
D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000378:metabolism / Q000494:pharmacology*; D000998:Antiviral Agents / Q000378:metabolism / Q000494:pharmacology*; D001798:Blood Proteins / Q000378:metabolism / Q000494:pharmacology*; D002478:Cells, Cultured; D006224:Cricetinae; D004285:Dogs; D006801:Humans; D053118:Influenza A Virus, H1N1 Subtype / Q000187:drug effects / Q000472:pathogenicity; D053122:Influenza A Virus, H3N2 Subtype / Q000187:drug effects / Q000472:pathogenicity; D053124:Influenza A Virus, H5N1 Subtype / Q000187:drug effects / Q000472:pathogenicity; D009980:Influenza A virus / Q000187:drug effects* / Q000472:pathogenicity*; D061985:Madin Darby Canine Kidney Cells; D009504:Neutrophils / Q000378:metabolism; D010446:Peptide Fragments / Q000494:pharmacology; D014779:Virus Replication / Q000187:drug effects
D023181:Antimicrobial Cationic Peptides; D000998:Antiviral Agents; D001798:Blood Proteins; D010446:Peptide Fragments; C021623:bactericidal permeability increasing protein