By Karl Maramorosch, Aaron J. Shatkin
The Advances in Virus examine sequence covers a various diversity of in-depth reports supplying a useful assessment of the present box of virology. This eclectic quantity includes six reports overlaying subject matters on the subject of plant viruses, evolution of viruses with hosts and mobilephone popularity by means of viruses.
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Additional info for Advances in Virus Research, Vol. 63
Whereas the HBV S domain contains additional cysteine residues, with those in the second hydrophilic, surface-exposed loop involved in mixed dimer formation between L, S, and M (Wunderlich and Bruss, 1996), the DHBV envelope proteins only contain the three cysteines in the first hydrophilic loop that are strictly conserved in all hepadnaviruses. These cysteines have been shown to be essential for secretion of HBV subviral particles (Mangold and Streeck, 1993); however, they do not form intermolecular disulfide bonds upon secretion from the cell.
5B). The mechanism underlying P* formation remains to be established. One option is that the C-terminal RNase H domain occludes the D" RNA binding site, which must reside between the TP and RT domains to allow simultaneous access to the template region of the priming Tyr-residue in TP and the polymerase active site in RT; Hsc70 may prevent this occlusion by altering the relative juxtapositions of the individual domains. Whether Hsc70 remains bound to the P protein during D" RNA binding and/or the subsequent initiation of DNA synthesis is not clear.
Clearly, the in vitro culture system is able to mimic some but not all the conditions conducive to efficient in vivo infection. Further studies, particularly of viral attachment and entry, may identify mechanisms that could be modulated to further enhance in vitro infection efficiency. 3. , 1998). , 1998). , 1995) may occur through steric hindrance (there are proportionally more S domain sites than preS) and not through binding to a membrane attachment site per se. Therefore, it is not clear whether multivalent binding of DHBV via an additional and perhaps sequential membrane interaction occurs with S and/or the S domain of L.