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J. Biol. Chem., Vol. 275, Issue 45, 34946-34953, November 10, 2000
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From the The envelope glycoprotein, gp160, of simian
immunodeficiency virus (SIV) shares ~25% sequence identity with
gp160 from the human immunodeficiency virus, type I, indicating a close
structural similarity. As a result of binding to cell surface CD4 and
co-receptor (e.g. CCR5 and CXCR4), both SIV and human
immunodeficiency virus gp160 mediate viral entry by membrane fusion. We
report here the characterization of gp160e, the soluble ectodomain of
SIV gp160. The ectodomain has been expressed in both insect cells and
Chinese hamster ovary (CHO)-Lec3.2.8.1 cells, deficient in enzymes
necessary for synthesizing complex oligosaccharides. Both the primary
and a secondary proteolytic cleavage sites between the gp120 and gp41 subunits of gp160 were mutated to prevent cleavage and shedding of
gp120. The purified, soluble glycoprotein is shown to be trimeric by
chemical cross-linking, gel filtration chromatography, and analytical
ultracentrifugation. It forms soluble, tight complexes with soluble CD4
and a number of Fab fragments from neutralizing monoclonal antibodies.
Soluble complexes were also produced of enzymatically deglycosylated
gp160e and of gp160e variants with deletions in the variable segments.
Expression, Purification, and Characterization of gp160e, the
Soluble, Trimeric Ectodomain of the Simian Immunodeficiency Virus
Envelope Glycoprotein, gp160*
,,
, and**
Laboratory of Molecular Medicine, The
Children's Hospital, Howard Hughes Medical Institute, Boston,
Massachusetts 02215, § Dana Farber Cancer Institute, Jimmy
Fund Bldg. 318, 44 Binney St., Boston, Massachusetts 02215, ¶ National Institute for Medical Research, The Ridgeway, Mill
Hill, London, NW7 1AA, United Kingdom
*
This research was supported by a special National Institutes
of Health Program for AIDS, the Innovation Grant Program for Approaches
in HIV Vaccines Research (to S. C. H. and D. C. W.), the Medical
Research Council (UK), Novel HIV Therapy-IPCP Grant AI43649 (to
E. R.), and the Howard Hughes Medical Institute (HHMI).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Investigator of the HHMI.
**
To whom correspondence should be addressed: Laboratory of Molecular
Medicine, The Children's Hospital, Howard Hughes Medical Institute,
320 Longwood Ave., Enders 673, Boston, MA 02215. Tel.: 617-355-7373;
Fax: 617-738-0184; E-mail: dcwadmin@crystal.harvard.edu.
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