Induction of heat-shock protein 70 by prostaglandin A1 inhibits HIV-1 Vif-mediated degradation of APOBEC3G

Ryuichi Sugiyama; Makoto Abe; Hironori Nishitsuji; Yuko Murakami; Hiroaki Takeuchi; Hiroshi Takaku

doi:10.1016/j.antiviral.2013.06.017

Induction of heat-shock protein 70 by prostaglandin A₁ inhibits HIV-1 Vif-mediated degradation of APOBEC3G

Ryuichi Sugiyama, Makoto Abe, Hironori Nishitsuji, Yuko Murakami, Hiroaki Takeuchi, Hiroshi Takaku

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

8 Citations (Scopus)

Abstract

Previous studies have demonstrated that cyclopentenone prostaglandins (cyPGs) inhibit human immunodeficiency virus type 1 (HIV-1) replication in various cell types. This antiviral activity has been associated with the induction of heat-shock protein 70 (HSP70) in infected cells. We investigated a new role of prostaglandin A₁ (PGA₁) in the replication of HIV-1 in non-permissive cells. Because overexpression of HSP70 blocks the viral infectivity factor (Vif)-mediated degradation of APOBEC3G (A3G) via the ubiquitin-proteasome pathway, we examined the effects of PGA₁ on A3G and HIV-1 replication. The induction of HSP70 synthesis by PGA₁ blocked Vif-mediated A3G degradation and enhanced the incorporation of A3G into both wild-type and Vif-deficient viruses. Furthermore, we determined the viral titer of HIV-1 particles produced from PGA₁-treated 293T cells. The induction of HSP70 synthesis by PGA₁ significantly reduced the viral titer in the presence of A3G. Additionally, the p24 Gag antigen levels were dramatically reduced in non-permissive cells treated once or repeatedly with PGA₁. Thus, we showed that PGA₁ inhibits HIV-1 replication, at least in part, by blocking Vif-mediated A3G degradation.

Original language	English
Pages (from-to)	307-311
Number of pages	5
Journal	Antiviral Research
Volume	99
Issue number	3
DOIs	https://doi.org/10.1016/j.antiviral.2013.06.017
Publication status	Published - 09-2013
Externally published	Yes

All Science Journal Classification (ASJC) codes

Pharmacology
Virology

UN SDGs

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

Access to Document

10.1016/j.antiviral.2013.06.017

Cite this

@article{2fe4afb0bb4b49e0b206960ddc9b1270,

title = "Induction of heat-shock protein 70 by prostaglandin A1 inhibits HIV-1 Vif-mediated degradation of APOBEC3G",

abstract = "Previous studies have demonstrated that cyclopentenone prostaglandins (cyPGs) inhibit human immunodeficiency virus type 1 (HIV-1) replication in various cell types. This antiviral activity has been associated with the induction of heat-shock protein 70 (HSP70) in infected cells. We investigated a new role of prostaglandin A1 (PGA1) in the replication of HIV-1 in non-permissive cells. Because overexpression of HSP70 blocks the viral infectivity factor (Vif)-mediated degradation of APOBEC3G (A3G) via the ubiquitin-proteasome pathway, we examined the effects of PGA1 on A3G and HIV-1 replication. The induction of HSP70 synthesis by PGA1 blocked Vif-mediated A3G degradation and enhanced the incorporation of A3G into both wild-type and Vif-deficient viruses. Furthermore, we determined the viral titer of HIV-1 particles produced from PGA1-treated 293T cells. The induction of HSP70 synthesis by PGA1 significantly reduced the viral titer in the presence of A3G. Additionally, the p24 Gag antigen levels were dramatically reduced in non-permissive cells treated once or repeatedly with PGA1. Thus, we showed that PGA1 inhibits HIV-1 replication, at least in part, by blocking Vif-mediated A3G degradation.",

keywords = "APOBEC3G, Antiviral, Heat-shock protein, Human immunodeficiency virus, Prostaglandin A, Viral infectivity factor",

author = "Ryuichi Sugiyama and Makoto Abe and Hironori Nishitsuji and Yuko Murakami and Hiroaki Takeuchi and Hiroshi Takaku",

note = "Funding Information: We thank Dr. Darlene Chen for providing pcDNA-A3G-HA and Haruki Naganuma and Hiroshi Koseki for their technical assistance. This work was supported in part by the following: a Grant-in-Aid for Science Research (C) from the Japan Society for the Promotion of Science (JSPS), Japan; a Grant-in-Aid for AIDS research from the Ministry of Health, Labor, and Welfare, Japan; and a Grant from the Strategic Research Foundation Grant-aided Project for Private Universities from the Ministry of Education, Culture, Sport, Science, and Technology, Japan (MEXT). ",

year = "2013",

month = sep,

doi = "10.1016/j.antiviral.2013.06.017",

language = "English",

volume = "99",

pages = "307--311",

journal = "Antiviral Research",

issn = "0166-3542",

publisher = "Elsevier B.V.",

number = "3",

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TY - JOUR

T1 - Induction of heat-shock protein 70 by prostaglandin A1 inhibits HIV-1 Vif-mediated degradation of APOBEC3G

AU - Sugiyama, Ryuichi

AU - Abe, Makoto

AU - Nishitsuji, Hironori

AU - Murakami, Yuko

AU - Takeuchi, Hiroaki

AU - Takaku, Hiroshi

N1 - Funding Information: We thank Dr. Darlene Chen for providing pcDNA-A3G-HA and Haruki Naganuma and Hiroshi Koseki for their technical assistance. This work was supported in part by the following: a Grant-in-Aid for Science Research (C) from the Japan Society for the Promotion of Science (JSPS), Japan; a Grant-in-Aid for AIDS research from the Ministry of Health, Labor, and Welfare, Japan; and a Grant from the Strategic Research Foundation Grant-aided Project for Private Universities from the Ministry of Education, Culture, Sport, Science, and Technology, Japan (MEXT).

PY - 2013/9

Y1 - 2013/9

N2 - Previous studies have demonstrated that cyclopentenone prostaglandins (cyPGs) inhibit human immunodeficiency virus type 1 (HIV-1) replication in various cell types. This antiviral activity has been associated with the induction of heat-shock protein 70 (HSP70) in infected cells. We investigated a new role of prostaglandin A1 (PGA1) in the replication of HIV-1 in non-permissive cells. Because overexpression of HSP70 blocks the viral infectivity factor (Vif)-mediated degradation of APOBEC3G (A3G) via the ubiquitin-proteasome pathway, we examined the effects of PGA1 on A3G and HIV-1 replication. The induction of HSP70 synthesis by PGA1 blocked Vif-mediated A3G degradation and enhanced the incorporation of A3G into both wild-type and Vif-deficient viruses. Furthermore, we determined the viral titer of HIV-1 particles produced from PGA1-treated 293T cells. The induction of HSP70 synthesis by PGA1 significantly reduced the viral titer in the presence of A3G. Additionally, the p24 Gag antigen levels were dramatically reduced in non-permissive cells treated once or repeatedly with PGA1. Thus, we showed that PGA1 inhibits HIV-1 replication, at least in part, by blocking Vif-mediated A3G degradation.

AB - Previous studies have demonstrated that cyclopentenone prostaglandins (cyPGs) inhibit human immunodeficiency virus type 1 (HIV-1) replication in various cell types. This antiviral activity has been associated with the induction of heat-shock protein 70 (HSP70) in infected cells. We investigated a new role of prostaglandin A1 (PGA1) in the replication of HIV-1 in non-permissive cells. Because overexpression of HSP70 blocks the viral infectivity factor (Vif)-mediated degradation of APOBEC3G (A3G) via the ubiquitin-proteasome pathway, we examined the effects of PGA1 on A3G and HIV-1 replication. The induction of HSP70 synthesis by PGA1 blocked Vif-mediated A3G degradation and enhanced the incorporation of A3G into both wild-type and Vif-deficient viruses. Furthermore, we determined the viral titer of HIV-1 particles produced from PGA1-treated 293T cells. The induction of HSP70 synthesis by PGA1 significantly reduced the viral titer in the presence of A3G. Additionally, the p24 Gag antigen levels were dramatically reduced in non-permissive cells treated once or repeatedly with PGA1. Thus, we showed that PGA1 inhibits HIV-1 replication, at least in part, by blocking Vif-mediated A3G degradation.

KW - APOBEC3G

KW - Antiviral

KW - Heat-shock protein

KW - Human immunodeficiency virus

KW - Prostaglandin A

KW - Viral infectivity factor

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