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Journal of Virology, June 2002, p. 6332-6343, Vol. 76, No. 12
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.12.6332-6343.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Envelope-Dependent, Cyclophilin-Independent Effects of Glycosaminoglycans on Human Immunodeficiency Virus Type 1 Attachment and Infection

Yi-jun Zhang,1,2 Theodora Hatziioannou,1,3,4 Trinity Zang,1,2 Douglas Braaten,5 Jeremy Luban,5 Stephen P. Goff,3,4 and Paul D. Bieniasz1,2*

Aaron Diamond AIDS Research Center,1 Rockefeller University,2 Department of Biochemistry and Molecular Biophysics,3 Department of Microbiology,5 Howard Hughes Medical Institute, Columbia University College of Physicians and Surgeons, New York, New York4

Received 12 December 2001/ Accepted 19 March 2002

Cell surface glycosaminoglycans (GAGs), in particular heparan sulfate (HS), have been proposed to mediate the attachment of human immunodeficiency virus type 1 (HIV-1) to target cells prior to virus entry, and both the viral gp120 envelope protein and virion-associated cyclophilin A (CypA) have been shown to directly interact with HS and its analogues. To determine the role of GAGs in HIV attachment and infection, we generated HIV-susceptible derivatives of CHO cell lines that either express high levels of GAGs (CHO-K1) or lack GAGs (pgsA745). Using a panel of HIV-1 envelopes, we found that cell surface GAG-mediated effects on virion attachment and infection vary in an envelope strain-dependent but coreceptor-independent manner. In fact, cell surface GAG-mediated enhancement of infection is confined to isolates that contain a highly positively charged V3-loop sequence, while infection by most strains is apparently inhibited by the presence of GAGs. Moreover, the enhancing and inhibitory effects of polycations and polyanions on HIV-1 infection are largely dependent on the presence of cell surface GAGs. These observations are consistent with a model in which GAGs influence in vitro HIV-1 infection primarily by modifying the charge characteristics of the target cell surface. Finally, the effects of GAGs on HIV-1 infection are observed to an equivalent extent whether CypA is present in or absent from virions. Overall, these data exclude a major role for GAGs in mediating the attachment of many HIV-1 strains to target cells via interactions with virion-associated gp120 or CypA.

* Corresponding author. Mailing address: Aaron Diamond AIDS Research Center, 455 First Ave., 7th Floor, New York, NY 10016. Phone: (212) 448-5070. Fax: (212) 448-5159. E-mail: pbienias{at}adarc.org.

Journal of Virology, June 2002, p. 6332-6343, Vol. 76, No. 12
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.12.6332-6343.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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