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.
Ishikawa
T
T
Department of Microbiology, University of California Medical Center, San Francisco 94143.
Kuroki
K
K
Lenhoff
R
R
Summers
J
J
Ganem
D
D
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