TY - JOUR
T1 - Cyclophilin B enhances HIV-1 infection
AU - DeBoer, Jason
AU - Madson, Christian J.
AU - Belshan, Michael
N1 - Funding Information:
This work was supported by Public Health Service grant AI080348 from the National Institute of Allergy and Infectious Diseases . Jason DeBoer is funded by the US Army ׳s Medical Service Corp Long Term Health Education Program. The following reagent was obtained through the NIH AIDS Reagent Program, Division of AIDS, NIAID, NIH: Human rIL-2 from Dr. Maurice Gately, Hoffmann-La Roche Inc. The authors also wish to thank John West for his critique of the manuscript and the Creighton University Molecular Biology Core Facility for support with the microscopy.
Funding Information:
This work was supported by Public Health Service grant AI080348 from the National Institute of Allergy and Infectious Diseases. Jason DeBoer is funded by the US Army''s Medical Service Corp Long Term Health Education Program. The following reagent was obtained through the NIH AIDS Reagent Program, Division of AIDS, NIAID, NIH: Human rIL-2 from Dr. Maurice Gately, Hoffmann-La Roche Inc. The authors also wish to thank John West for his critique of the manuscript and the Creighton University Molecular Biology Core Facility for support with the microscopy.
Publisher Copyright:
© 2015 Elsevier Inc.
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 2016/2/1
Y1 - 2016/2/1
N2 - Cyclophilin B (CypB) is a member of the immunophilin family and intracellular chaperone. It predominantly localizes to the ER, but also contains a nuclear localization signal and is secreted from cells. CypB has been shown to interact with the Gag protein of human immunodeficiency type 1 (HIV-1). Several proteomic and genetic studies identified it as a potential factor involved in HIV replication. Herein, we show that over-expression of CypB enhances HIV infection by increasing nuclear import of viral DNA. This enhancement was unaffected by cyclosporine treatment and requires the N-terminus of the protein. The N-terminus contains an ER leader sequence, putative nuclear localization signal, and is required for secretion. Deletion of the N-terminus resulted in mislocalization from the ER and suppression of HIV infection. Passive transfer experiments showed that secreted CypB did not impact HIV infection. Combined, these experiments show that intracellular CypB modulates a pathway of HIV nuclear import.
AB - Cyclophilin B (CypB) is a member of the immunophilin family and intracellular chaperone. It predominantly localizes to the ER, but also contains a nuclear localization signal and is secreted from cells. CypB has been shown to interact with the Gag protein of human immunodeficiency type 1 (HIV-1). Several proteomic and genetic studies identified it as a potential factor involved in HIV replication. Herein, we show that over-expression of CypB enhances HIV infection by increasing nuclear import of viral DNA. This enhancement was unaffected by cyclosporine treatment and requires the N-terminus of the protein. The N-terminus contains an ER leader sequence, putative nuclear localization signal, and is required for secretion. Deletion of the N-terminus resulted in mislocalization from the ER and suppression of HIV infection. Passive transfer experiments showed that secreted CypB did not impact HIV infection. Combined, these experiments show that intracellular CypB modulates a pathway of HIV nuclear import.
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U2 - 10.1016/j.virol.2015.12.015
DO - 10.1016/j.virol.2015.12.015
M3 - Article
C2 - 26774171
AN - SCOPUS:84954214976
VL - 489
SP - 282
EP - 291
JO - Virology
JF - Virology
SN - 0042-6822
ER -