Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B

Jeremy Luban; Karen Leigh Bossolt; Ettaly K. Franke; Ganjam V. Kalpana; Stephen P. Goff

doi:10.1016/0092-8674(93)90637-6

Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B

Jeremy Luban, Karen Leigh Bossolt, Ettaly K. Franke, Ganjam V. Kalpana, Stephen P. Goff

Research output: Contribution to journal › Article › peer-review

727 Scopus citations

Abstract

Retroviral Gag protein is capable of directing the assembly of virion particles independent of other retroviral elements and plays an important role early in the infection of a cell. Using the GAL4 two hybrid system, we screened a cDNA expression library and identified two host proteins, cyclophillns (CyPs) A and B, which interact specifically with the human immunodeficiency virus type 1 (HIV-1) Gag polyprotein Pr55^gag. Glutathione S-transferase-CyP fusion proteins bind tightly to Pr55^gag in vitro, as well as to the HIV-1 capsid protein p24. Cyclosporin A efficiently disrupts the Gag-CyPA interaction and less efficiently disrupts the Gag-CyPB interaction. The Gag-CyP interaction may be important for the HIV-1 life cycle and may be relevant to the pathology caused by this immunosuppressive virus.

Original language	English (US)
Pages (from-to)	1067-1078
Number of pages	12
Journal	Cell
Volume	73
Issue number	6
DOIs	https://doi.org/10.1016/0092-8674(93)90637-6
State	Published - Jun 18 1993
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/0092-8674(93)90637-6

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title = "Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B",

abstract = "Retroviral Gag protein is capable of directing the assembly of virion particles independent of other retroviral elements and plays an important role early in the infection of a cell. Using the GAL4 two hybrid system, we screened a cDNA expression library and identified two host proteins, cyclophillns (CyPs) A and B, which interact specifically with the human immunodeficiency virus type 1 (HIV-1) Gag polyprotein Pr55gag. Glutathione S-transferase-CyP fusion proteins bind tightly to Pr55gag in vitro, as well as to the HIV-1 capsid protein p24. Cyclosporin A efficiently disrupts the Gag-CyPA interaction and less efficiently disrupts the Gag-CyPB interaction. The Gag-CyP interaction may be important for the HIV-1 life cycle and may be relevant to the pathology caused by this immunosuppressive virus.",

author = "Jeremy Luban and Bossolt, {Karen Leigh} and Franke, {Ettaly K.} and Kalpana, {Ganjam V.} and Goff, {Stephen P.}",

note = "Funding Information: The authors especially wish to thank Stanley Fields and Paul Bartel for their generous contribution of reagents and for technical assistance. We would also like to thank Ulla Beauchamp, Marian Carlson, Jakob Franke, Christopher F. J. Hardy, E. Jane Albert Hubbard, David Shore, and Xiaolu Yang for helpful discussions, technical assistance, and assistance with the manuscript. Dag Helland, Eric Hunter, Patrick B. Johnston, and Sun S. Rheecontributed needed reagents. This work was supported by grant Al 24845 from the National Institute of Allergy and Infectious Diseases (NIAID) to S. P. G., and by grant Al 00988 from the NIAID and grant 91-49 from the James S. McDonnell Foundation to J. L. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.",

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doi = "10.1016/0092-8674(93)90637-6",

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AU - Luban, Jeremy

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AU - Franke, Ettaly K.

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AU - Goff, Stephen P.

N1 - Funding Information: The authors especially wish to thank Stanley Fields and Paul Bartel for their generous contribution of reagents and for technical assistance. We would also like to thank Ulla Beauchamp, Marian Carlson, Jakob Franke, Christopher F. J. Hardy, E. Jane Albert Hubbard, David Shore, and Xiaolu Yang for helpful discussions, technical assistance, and assistance with the manuscript. Dag Helland, Eric Hunter, Patrick B. Johnston, and Sun S. Rheecontributed needed reagents. This work was supported by grant Al 24845 from the National Institute of Allergy and Infectious Diseases (NIAID) to S. P. G., and by grant Al 00988 from the NIAID and grant 91-49 from the James S. McDonnell Foundation to J. L. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.

PY - 1993/6/18

Y1 - 1993/6/18

N2 - Retroviral Gag protein is capable of directing the assembly of virion particles independent of other retroviral elements and plays an important role early in the infection of a cell. Using the GAL4 two hybrid system, we screened a cDNA expression library and identified two host proteins, cyclophillns (CyPs) A and B, which interact specifically with the human immunodeficiency virus type 1 (HIV-1) Gag polyprotein Pr55gag. Glutathione S-transferase-CyP fusion proteins bind tightly to Pr55gag in vitro, as well as to the HIV-1 capsid protein p24. Cyclosporin A efficiently disrupts the Gag-CyPA interaction and less efficiently disrupts the Gag-CyPB interaction. The Gag-CyP interaction may be important for the HIV-1 life cycle and may be relevant to the pathology caused by this immunosuppressive virus.

AB - Retroviral Gag protein is capable of directing the assembly of virion particles independent of other retroviral elements and plays an important role early in the infection of a cell. Using the GAL4 two hybrid system, we screened a cDNA expression library and identified two host proteins, cyclophillns (CyPs) A and B, which interact specifically with the human immunodeficiency virus type 1 (HIV-1) Gag polyprotein Pr55gag. Glutathione S-transferase-CyP fusion proteins bind tightly to Pr55gag in vitro, as well as to the HIV-1 capsid protein p24. Cyclosporin A efficiently disrupts the Gag-CyPA interaction and less efficiently disrupts the Gag-CyPB interaction. The Gag-CyP interaction may be important for the HIV-1 life cycle and may be relevant to the pathology caused by this immunosuppressive virus.

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Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B

Abstract

ASJC Scopus subject areas

UN SDGs

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