A. Ciervo et al., POLYPEPTIDE 3AB OF HEPATITIS-A VIRUS IS A TRANSMEMBRANE PROTEIN, Biochemical and biophysical research communications (Print), 249(1), 1998, pp. 266-274
Hepatitis A virus (HAV) protein 3AB is a membrane-interacting protein
containing a stretch of 21 hydrophobic amino acid residues. The nature
of its membrane association was studied in detail by analysing variou
s deletion mutants. In vivo and in vitro expression of the wild-type p
rotein and its mutants allowed to demonstrate that the hydrophobic dom
ain interacts with membranes and to define the portions essential for
this feature. Furthermore, the results suggest that 3AB behaves as an
integral membrane protein. Expression in Escherichia coil showed that
3AB can be isolated, in association with membranes, both in monomeric
and in dimeric form. This finding was confirmed in vitro after post-tr
anslational incubation of the protein with microsomal membranes. Analy
sis of deletion mutants demonstrated that the dimerization region colo
calises with the hydrophobic transmembrane domain, implicating that HA
V 3AB could form oligomers mediated by the interaction of transmembran
e alpha-helices. (C) 1998 Academic Press.