Identification of a prenylation site in delta virus large antigen
JS Glenn, JA Watson, CM Havel, JM White - Science, 1992 - science.org
JS Glenn, JA Watson, CM Havel, JM White
Science, 1992•science.orgDuring replication, hepatitis delta virus (HDV) switches from production of small to large
delta antigen. Both antigen isoforms have an HDV genome binding domain and are
packaged into hepatitis B virus (HBV)-derived envelopes but differ at their carboxyl termini.
The large antigen was shown to contain a terminal CXXX box and undergo prenylation. The
large, but not the small, antigen formed secreted particles when expressed singly with HBV
surface antigen. Mutation of Cys211 in the CXXX box of the large antigen abolished both …
delta antigen. Both antigen isoforms have an HDV genome binding domain and are
packaged into hepatitis B virus (HBV)-derived envelopes but differ at their carboxyl termini.
The large antigen was shown to contain a terminal CXXX box and undergo prenylation. The
large, but not the small, antigen formed secreted particles when expressed singly with HBV
surface antigen. Mutation of Cys211 in the CXXX box of the large antigen abolished both …
During replication, hepatitis delta virus (HDV) switches from production of small to large delta antigen. Both antigen isoforms have an HDV genome binding domain and are packaged into hepatitis B virus (HBV)-derived envelopes but differ at their carboxyl termini. The large antigen was shown to contain a terminal CXXX box and undergo prenylation. The large, but not the small, antigen formed secreted particles when expressed singly with HBV surface antigen. Mutation of Cys211 in the CXXX box of the large antigen abolished both prenylation and particle formation, suggesting that this site is important for virion morphogenesis.
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