West Nile virus is neutralized by HOCl-modified human serum albumin that binds to domain III of the viral envelope protein E.
The outbreaks of West Nile virus (WNV), an emerging flavivirus recently implicated in outbreaks of fatal encephalitis, necessitate the development of effective anti-WNV drugs. In this study, it is demonstrated that human serum albumin is transformed into a WNV antiviral substance by hypochlorite (HOCl) modification. The HOCl-modified albumin efficiently neutralized WNV in vitro (EC50=300 nM) and showed binding to a recombinant protein, representing the domain III of the WNV external envelope E glycoprotein.
Vossmann
Markus
M
Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard Nocht Str. 74, 20359 Hamburg, Germany. markus.vossmann@ge.com
Kirst
Martin
M
Ludolfs
Diana
D
Schreiber
Michael
M
D000818:Animals; D001665:Binding Sites; D049109:Cell Proliferation / Q000187:drug effects; D002522:Chlorocebus aethiops; D006801:Humans; D006997:Hypochlorous Acid / Q000494:pharmacology; D066298:In Vitro Techniques; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000737:chemistry / Q000494:pharmacology*; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism; D010948:Viral Plaque Assay; D014774:Virulence / Q000187:drug effects; D014779:Virus Replication / Q000187:drug effects; D014902:West Nile virus / Q000187:drug effects* / Q000472:pathogenicity / Q000502:physiology
D012709:Serum Albumin; D014759:Viral Envelope Proteins; D006997:Hypochlorous Acid