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Journal of Virology, June 1999, p. 4640-4650, Vol. 73, No. 6
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Cross-Subtype Neutralizing Antibodies Induced in
Baboons by a Subtype E gp120 Immunogen Based on an R5 Primary Human
Immunodeficiency Virus Type 1 Envelope
Thomas C.
VanCott,1,*
John R.
Mascola,2,3
Lawrence D.
Loomis-Price,1
Faruk
Sinangil,4
Naamah
Zitomersky,1
John
McNeil,2
Merlin L.
Robb,2
Deborah L.
Birx,2 and
Susan
Barnett4
Henry M. Jackson
Foundation1 and Division of
Retrovirology, Walter Reed Army Institute of
Research,2 Rockville, Maryland 20850;
Department of Infectious Diseases, Naval Medical Research
Institute, Bethesda, Maryland 208923; and
Chiron Corporation, Emeryville, California
946084
Received 28 December 1998/Accepted 1 March 1999
Global human immunodeficiency virus type 1 (HIV-1) diversity may
require engineering vaccines to express antigens representing strains
prevalent in the target population of vaccine testing. The majority
(90%) of incident infections in Thailand are genetic subtype E, with a small percentage of subtype B infections in the
intravenous drug user populations. We have evaluated and compared the binding and HIV-1 neutralizing properties of serum
antibodies induced in baboons by CHO cell-expressed monomeric gp120
derived from a CCR5-using (R5) subtype E primary
HIV-1CM235 or a CXCR4-using (X4) subtype B T-cell
line-adapted (TCLA) HIV-1SF2 isolate. In contrast
to the subtype-specific HIV-1 neutralizing antibodies induced with
recombinant HIV-1SF2 gp120
(rgp120SF2), rgp120CM235 immunization induced
antibodies capable of neutralizing both subtype E and subtype B TCLA
HIV-1 isolates. However, neither immunogen induced antibodies capable
of neutralizing primary HIV-1 isolates. Antibody induced by
rgp120CM235 preferentially bound natively folded gp120 and
retained strong cross-reactivity against multiple gp120 strains within
subtype E as well as subtype B. In contrast, antibody
responses to rgp120SF2 were directed predominantly to linear epitopes poorly exposed on native gp120 and had more limited cross-recognition of divergent gp120. Fine epitope mapping revealed differences in antibody specificities. While both
rgp120CM235 and rgp120SF2 induced antibodies to
regions within C1, V1/V2, V3, and C5, unique responses were induced by
rgp120CM235 to multiple epitopes within C2 and by
rgp120SF2 to multiple epitopes within C3, V4, and C4. These
data demonstrate that strain and/or phenotypic differences of HIV-1
subunit gp120 immunogens can substantially alter antibody binding
specificities and subsequent HIV-1 neutralizing capacity.
*
Corresponding author. Mailing address: Henry M. Jackson
Foundation, 13 Taft Ct., Suite 200, Rockville, MD 20850. Phone: (301) 762-0089. Fax: (301) 762-4177. E-mail address:
tvancott{at}hiv.hjf.org.
Journal of Virology, June 1999, p. 4640-4650, Vol. 73, No. 6
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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