Analysis of the binding of a host cell surface glycoprotein to the preS protein of duck hepatitis B virus.
We have previously identified a 180-kDa host cell glycoprotein (gp180) that specifically binds the surface envelope of duck hepatitis B virus (DHBV) and whose binding is inhibited by neutralizing antiviral monoclonal antibodies. Here we map the viral determinants required for gp180 binding to a 66-amino acid region within the preS domain of the envelope coding region. This region includes both major neutralizing preS epitopes previously defined by monoclonal antibodies. Examination of a series of linker-substitution mutations throughout preS indicates that all mutations that block gp180 binding ablate virus infectivity. Interestingly, two mutations that do not prevent binding can also impair infectivity.
Department of Microbiology, University of California Medical Center, San Francisco 94143.
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T
Ishikawa
K
K
Kuroki
R
R
Lenhoff
J
J
Summers
D
D
Ganem
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004372:Ducks / Q000382:microbiology; D006514:Hepatitis B Surface Antigens / Q000737:chemistry; D004371:Hepatitis Virus, Duck / Q000378:metabolism*; D006518:Hepatitis Viruses / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D011991:Receptors, Virus / Q000378:metabolism*; D011993:Recombinant Fusion Proteins; D013329:Structure-Activity Relationship; D014759:Viral Envelope Proteins / Q000378:metabolism*
D006514:Hepatitis B Surface Antigens; D008562:Membrane Glycoproteins; D011991:Receptors, Virus; D011993:Recombinant Fusion Proteins; D014759:Viral Envelope Proteins