Hepatitis B virus infection is primarily mediated by the interaction of the preS region of the viral envelope protein with its still unknown cellular receptor. Using recombinantly expressed preS proteins, the distribution of preS-binding receptors on cell lines from extra-hepatic origins was determined by immunofluorescence and flow cytometry. In contrast to human liver cell lines, most cell lines from extrahepatic origins did not bind preS proteins. Nevertheless, exceptions were found in the bone marrow, derived cell line, KG-1, and the osteogenic sarcoma cell line SaOS-2, as well as in the previously reported EBV-transformed B-cell line, Wa. To determine the biochemical nature of these receptors, Wa-cells were cell surface biotinylated an...
Using a solid-phase assay we have demonstrated specific competition between the preS1 sequence of he...
The preS1 domain of hepatitis B virus envelope proteins contains a site of attachment to the hepatoc...
The N-terminal portion of the large envelope protein of the human hepatitis B virus (HBV), the preS1...
Hepatitis B virus infection is primarily mediated by the interaction of the preS region of the viral...
Specific attachment onto the target cell is one of the mechanisms that causes the restricted and spe...
Viral surface proteins are known to play an essential role in attachment of the virus particle to th...
One of the essential functions of virus surface proteins is the recognition of specific receptors on...
It has been suggested that hepatitis B virus (HBV) binds to a receptor on the plasma membrane of hum...
It has been suggested that hepatitis B virus (HBV) binds to a receptor on the plasma membrane of hum...
.A direct involvement of the hepatitis B virus (HBV) preS1-(21-47) sequence in virus attachment to c...
As a hepatitis B virus (HBV) envelope domain, preS plays significant roles in receptor recognition a...
Attachment of hepatitis B virus to a hepatoblastoma cell line (HepG2) was examined using a synthetic...
A quantitative assay of hepatitis B virus (HBV) binding to hepatocyte plasma membranes was adapted t...
The surface antigen of hepatitis B virus (HBsAg) exposes three protein domains: preS1, preS2, and S....
Using a solid-phase assay we have demonstrated specific competition between the preS1 sequence of he...
Using a solid-phase assay we have demonstrated specific competition between the preS1 sequence of he...
The preS1 domain of hepatitis B virus envelope proteins contains a site of attachment to the hepatoc...
The N-terminal portion of the large envelope protein of the human hepatitis B virus (HBV), the preS1...
Hepatitis B virus infection is primarily mediated by the interaction of the preS region of the viral...
Specific attachment onto the target cell is one of the mechanisms that causes the restricted and spe...
Viral surface proteins are known to play an essential role in attachment of the virus particle to th...
One of the essential functions of virus surface proteins is the recognition of specific receptors on...
It has been suggested that hepatitis B virus (HBV) binds to a receptor on the plasma membrane of hum...
It has been suggested that hepatitis B virus (HBV) binds to a receptor on the plasma membrane of hum...
.A direct involvement of the hepatitis B virus (HBV) preS1-(21-47) sequence in virus attachment to c...
As a hepatitis B virus (HBV) envelope domain, preS plays significant roles in receptor recognition a...
Attachment of hepatitis B virus to a hepatoblastoma cell line (HepG2) was examined using a synthetic...
A quantitative assay of hepatitis B virus (HBV) binding to hepatocyte plasma membranes was adapted t...
The surface antigen of hepatitis B virus (HBsAg) exposes three protein domains: preS1, preS2, and S....
Using a solid-phase assay we have demonstrated specific competition between the preS1 sequence of he...
Using a solid-phase assay we have demonstrated specific competition between the preS1 sequence of he...
The preS1 domain of hepatitis B virus envelope proteins contains a site of attachment to the hepatoc...
The N-terminal portion of the large envelope protein of the human hepatitis B virus (HBV), the preS1...