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Minder, D; Böni, J; Schüpbach, J; Gehring, H (2002). Immunophilins and HIV-1 infection. Archives of Virology, 147(8):1531-1542.

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Abstract

Peptides of the V3 loop of the HIV-1 envelope glycoprotein gp120 have been shown to bind with high affinity to the immunophilins cyclophilin (Cyp) A, CypB and the FK506-binding protein 12 (FKBP12) [10]. We investigated whether immunophilins affect HIV-1 infection by assuming they are able to bind to the V3 loop of gp120. T cells and peripheral blood mononuclear cells were infected with T-cell-tropic or macrophage-tropic HIV-1 strains, respectively, in the presence of different concentrations of immunophilins. P24 antigen ELISA and real-time PCR measurements demonstrated that exogenously added immunophilins do not influence HIV-1 infection. CypA is known to interact with the HIV-1 Gag polyprotein and to be incorporated into the virions. This incorporation can be prevented by cyclosporin A (CsA) resulting in a decreased yield of infectious virus, the mechanism of which is unknown. We measured a normal production of proviral DNA in the first round of infection in CsA treated cells but afterwards, infection was decreased if CsA was present. Pre-treatment of the HIV-1 inocula with CsA, blocking the function of virus-associated CypA, did not inhibit the ensuing yield of infection. We therefore may conclude that endogenous CypA exerts its action after reverse transcription but before virus maturation, probably during capsid formation. FK520, an immunosuppressor which binds to FKBP, had no effect on HIV-1 infection.

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
DDC:570 Life sciences; biology
Language:English
Date:1 August 2002
Deposited On:11 Feb 2008 12:20
Last Modified:27 Nov 2013 20:26
Publisher:Springer
ISSN:0304-8608
Publisher DOI:10.1007/s00705-002-0826-2
PubMed ID:12181673
Citations:Web of Science®. Times Cited: 10
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