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Journal of Virology, May 2001, p. 4208-4218, Vol. 75, No. 9
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.9.4208-4218.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Envelope Glycoprotein Determinants of Neutralization Resistance
in a Simian-Human Immunodeficiency Virus (SHIV-HXBc2P 3.2) Derived
by Passage in Monkeys
Zhihai
Si,1
Mark
Cayabyab,1 and
Joseph
Sodroski1,2,*
Department of Cancer Immunology and AIDS,
Dana-Farber Cancer Institute, Department of Pathology, Harvard
Medical School,1 and Department of
Immunology and Infectious Diseases, Harvard School of Public
Health,2 Boston, Massachusetts 02115
Received 27 December 2000/Accepted 6 February 2001
The simian-human immunodeficiency virus SHIV-HXBc2 contains
the envelope glycoproteins of a laboratory-adapted,
neutralization-sensitive human immunodeficiency virus type 1 variant,
HXBc2. Serial in vivo passage of the nonpathogenic SHIV-HXBc2
generated SHIV KU-1, which causes rapid CD4+ T-cell
depletion and an AIDS-like illness in monkeys. A molecularly cloned
pathogenic SHIV, SHIV-HXBc2P 3.2, was derived from the SHIV KU-1
isolate and differs from the parental SHIV-HXBc2 by only 12 envelope
glycoprotein amino acid residues. Relative to SHIV-HXBc2, SHIV-HXBc2P
3.2 was resistant to neutralization by all of the antibodies tested
with the exception of the 2G12 antibody. The sequence changes
responsible for neutralization resistance were located in variable
regions of the gp120 exterior envelope glycoprotein and in the gp41
transmembrane envelope glycoprotein. The 2G12 antibody, which
neutralized SHIV-HXBc2 and SHIV-HXBc2P 3.2 equally, bound the HXBc2 and
HXBc2P 3.2 envelope glycoproteins on the cell surface comparably.
The ability of the other tested antibodies to achieve saturation was
less for the HXBc2P 3.2 envelope glycoproteins than for the HXBc2
envelope glycoproteins, even though the affinity of the antibodies for
the two envelope glycoproteins was similar. Thus, a highly
neutralization-sensitive SHIV, by modifying both gp120 and gp41
glycoproteins, apparently achieves a neutralization-resistant state by
decreasing the saturability of its envelope glycoproteins by antibodies.
*
Corresponding author. Mailing address: Dana-Farber
Cancer Institute, 44 Binney St., JFB 824, Boston, MA 02115. Phone:
(617) 632-3371. Fax: (617) 632-4338. E-mail:
joseph_sodroski{at}dfci.harvard.edu.
Journal of Virology, May 2001, p. 4208-4218, Vol. 75, No. 9
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.9.4208-4218.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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