Conserved structural features in the interaction between retroviral surface and transmembrane glycoproteins?
Conserved structural features in the interaction between retroviral surface and transmembrane glycoproteins?
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逆转录病毒表面和跨膜糖蛋白之间相互作用的保守结构特征?
DOI:
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发表时间:
1992
影响因子:
1.5
通讯作者:
J. P. Moore
中科院分区:
文献类型:
--
作者:
Thomas F. Schulz;Bradford A. Jameson;Lucia Lopalco;Antonio G. Siccardi;Robin A. Weiss;J. P. Moore
Among the retroviruses, the surface (SU) and transmembrane (TM) glycoproteins of lentiviruses are linked exclusively by noncovalent bonds. For some C-type retroviruses, however, a small proportion of the SU proteins has been shown to be linked to their TM proteins by a disulfide bond, with the remainder being noncovalently associated. A region near the carboxyl terminus of the HIV-1 SU glycoprotein has been implicated in contacting the TM glycoprotein. Computer modelling indicates that this region of divergent lentivirus and oncovirus SU glycoproteins forms a structurally conserved "pocket" which could accommodate a "knob"-like protrusion formed by an immunodominant region in the TM protein containing the CxxxxxC (lentiviruses) or CxxxxxxCC (C- and D-type viruses) motif. An anti-idiotypic monoclonal antibody, raised against a monoclonal antibody reacting with a sequence in the "pocket" of HIV-1 gp120, was found to bind to synthetic peptides close to the CxxxxxC motif. It is suggested that part of the SU-TM linkage mechanism for the lentiviruses and oncoviruses is a 'knob and socket' structure and that the interaction between SU and TM proteins is similar in one region for lentiviruses and C-type as well as D-type viruses. The conserved knob and socket linkage may be relevant to a mechanism for viral-cell membrane fusion that is broadly common to all of these retroviruses.
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