LOCALIZATION OF THE LABILE DISULFIDE BOND BETWEEN SU AND TM OF THE MURINE LEUKEMIA-VIRUS ENVELOPE PROTEIN COMPLEX TO A HIGHLY CONSERVED CWLC MOTIF IN SU THAT RESEMBLES THE ACTIVE-SITE SEQUENCE OF THIOL-DISULFIDE EXCHANGE ENZYMES
A. Pinter et al., LOCALIZATION OF THE LABILE DISULFIDE BOND BETWEEN SU AND TM OF THE MURINE LEUKEMIA-VIRUS ENVELOPE PROTEIN COMPLEX TO A HIGHLY CONSERVED CWLC MOTIF IN SU THAT RESEMBLES THE ACTIVE-SITE SEQUENCE OF THIOL-DISULFIDE EXCHANGE ENZYMES, Journal of virology, 71(10), 1997, pp. 8073-8077
Previous studies have indicated that the surface (SU) and transmembran
e (TM) subunits of the envelope protein (Env) of murine leukemia virus
es (MuLVs) are joined by a labile disulfide bond that can be stabilize
d by treatment of virions with thiol-specific reagents. In the present
study this observation was extended to the Envs of additional classes
of MuLV, and the cysteines of SU involved in this linkage were mapped
by proteolytic fragmentation analyses to the CWLC sequence present at
the beginning of the C-terminal domain of SU. This sequence is highly
conserved across a broad range of distantly related retroviruses and
resembles the CXXC motif present at the active site of thiol-disulfide
exchange enzymes. A model is proposed in which rearrangements of the
SU-TM intersubunit disulfide linkage, mediated by the CWLC sequence, p
lay roles in the assembly and function of the Env complex.