Biosynthesis of hepatitis B virus e antigen: directed mutagenesis of the putative aspartyl protease site

التفاصيل البيبلوغرافية
العنوان: Biosynthesis of hepatitis B virus e antigen: directed mutagenesis of the putative aspartyl protease site
المؤلفون: Jean-Jean, O, Salhi, S, Carlier, D, Elie, C, De Recondo, A M, Rossignol, J M
المصدر: The Journal of Virology; December 1989, Vol. 63 Issue: 12 p5497-5500, 4p
مستخلص: The C gene products of all mammalian hepadnaviruses contain a region with sequence similarities to the catalytic center of the aspartyl proteases. This region could have the capacity to cleave precore proteins, leading to the synthesis of e antigen. By site-directed mutagenesis on a plasmid containing the hepatitis B virus C gene, we have replaced either the Asp residue of the putative aspartyl protease catalytic center or an Asp residue located 3 amino acids upstream. Transient expression of the mutated hepatitis B virus C gene in human and mouse cells showed that none of these mutations prevented the secretion of an accurately processed HBe antigen. Thus, we demonstrated that the aspartyl protease responsible for e antigen precursor processing is not C gene encoded but is more likely to be a cellular enzyme. From these results, we suggest a model for the mechanism of e antigen synthesis.
قاعدة البيانات: Supplemental Index
الوصف
تدمد:0022538X
10985514
DOI:10.1128/jvi.63.12.5497-5500.1989