Membrane-associated RING-CH (MARCH) 1 and 2 are MARCH family members that inhibit HIV-1 infection
Membrane-associated RING-CH 8 (MARCH8) is one of 11 members of the MARCH family of RING finger E3 ubiquitin ligases and down-regulates several membrane proteins (e.g. major histocompatibility complex II [MHC-II], CD86, and transferrin receptor). We recently reported that MARCH8 also targets HIV-1 en...
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| Published in | The Journal of biological chemistry Vol. 294; no. 10; pp. 3397 - 3405 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
Elsevier Inc
08.03.2019
American Society for Biochemistry and Molecular Biology |
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| Abstract | Membrane-associated RING-CH 8 (MARCH8) is one of 11 members of the MARCH family of RING finger E3 ubiquitin ligases and down-regulates several membrane proteins (e.g. major histocompatibility complex II [MHC-II], CD86, and transferrin receptor). We recently reported that MARCH8 also targets HIV-1 envelope glycoproteins and acts as an antiviral factor. However, it remains unclear whether other family members might have antiviral functions similar to those of MARCH8. Here we show that MARCH1 and MARCH2 are MARCH family members that reduce virion incorporation of envelope glycoproteins. Infectivity assays revealed that MARCH1 and MARCH2 dose-dependently suppress viral infection. Treatment with type I interferon enhanced endogenous expression levels of MARCH1 and MARCH2 in monocyte-derived macrophages. Expression of these proteins in virus-producing cells decreased the efficiency of viral entry and down-regulated HIV-1 envelope glycoproteins from the cell surface, resulting in reduced incorporation of envelope glycoproteins into virions, as observed in MARCH8 expression. With the demonstration that MARCH1 and MARCH2 are antiviral MARCH family members as presented here, these two proteins join a growing list of host factors that inhibit HIV-1 infection. |
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| AbstractList | Membrane-associated RING-CH 8 (MARCH8) is one of 11 members of the MARCH family of RING finger E3 ubiquitin ligases and down-regulates several membrane proteins (e.g. major histocompatibility complex II [MHC-II], CD86, and transferrin receptor). We recently reported that MARCH8 also targets HIV-1 envelope glycoproteins and acts as an antiviral factor. However, it remains unclear whether other family members might have antiviral functions similar to those of MARCH8. Here we show that MARCH1 and MARCH2 are MARCH family members that reduce virion incorporation of envelope glycoproteins. Infectivity assays revealed that MARCH1 and MARCH2 dose-dependently suppress viral infection. Treatment with type I interferon enhanced endogenous expression levels of MARCH1 and MARCH2 in monocyte-derived macrophages. Expression of these proteins in virus-producing cells decreased the efficiency of viral entry and down-regulated HIV-1 envelope glycoproteins from the cell surface, resulting in reduced incorporation of envelope glycoproteins into virions, as observed in MARCH8 expression. With the demonstration that MARCH1 and MARCH2 are antiviral MARCH family members as presented here, these two proteins join a growing list of host factors that inhibit HIV-1 infection.Membrane-associated RING-CH 8 (MARCH8) is one of 11 members of the MARCH family of RING finger E3 ubiquitin ligases and down-regulates several membrane proteins (e.g. major histocompatibility complex II [MHC-II], CD86, and transferrin receptor). We recently reported that MARCH8 also targets HIV-1 envelope glycoproteins and acts as an antiviral factor. However, it remains unclear whether other family members might have antiviral functions similar to those of MARCH8. Here we show that MARCH1 and MARCH2 are MARCH family members that reduce virion incorporation of envelope glycoproteins. Infectivity assays revealed that MARCH1 and MARCH2 dose-dependently suppress viral infection. Treatment with type I interferon enhanced endogenous expression levels of MARCH1 and MARCH2 in monocyte-derived macrophages. Expression of these proteins in virus-producing cells decreased the efficiency of viral entry and down-regulated HIV-1 envelope glycoproteins from the cell surface, resulting in reduced incorporation of envelope glycoproteins into virions, as observed in MARCH8 expression. With the demonstration that MARCH1 and MARCH2 are antiviral MARCH family members as presented here, these two proteins join a growing list of host factors that inhibit HIV-1 infection. Membrane-associated RING-CH 8 (MARCH8) is one of 11 members of the MARCH family of RING finger E3 ubiquitin ligases and down-regulates several membrane proteins ( e.g. major histocompatibility complex II [MHC-II], CD86, and transferrin receptor). We recently reported that MARCH8 also targets HIV-1 envelope glycoproteins and acts as an antiviral factor. However, it remains unclear whether other family members might have antiviral functions similar to those of MARCH8. Here we show that MARCH1 and MARCH2 are MARCH family members that reduce virion incorporation of envelope glycoproteins. Infectivity assays revealed that MARCH1 and MARCH2 dose-dependently suppress viral infection. Treatment with type I interferon enhanced endogenous expression levels of MARCH1 and MARCH2 in monocyte-derived macrophages. Expression of these proteins in virus-producing cells decreased the efficiency of viral entry and down-regulated HIV-1 envelope glycoproteins from the cell surface, resulting in reduced incorporation of envelope glycoproteins into virions, as observed in MARCH8 expression. With the demonstration that MARCH1 and MARCH2 are antiviral MARCH family members as presented here, these two proteins join a growing list of host factors that inhibit HIV-1 infection. Membrane-associated RING-CH 8 (MARCH8) is one of 11 members of the MARCH family of RING finger E3 ubiquitin ligases and down-regulates several membrane proteins ( major histocompatibility complex II [MHC-II], CD86, and transferrin receptor). We recently reported that MARCH8 also targets HIV-1 envelope glycoproteins and acts as an antiviral factor. However, it remains unclear whether other family members might have antiviral functions similar to those of MARCH8. Here we show that MARCH1 and MARCH2 are MARCH family members that reduce virion incorporation of envelope glycoproteins. Infectivity assays revealed that MARCH1 and MARCH2 dose-dependently suppress viral infection. Treatment with type I interferon enhanced endogenous expression levels of MARCH1 and MARCH2 in monocyte-derived macrophages. Expression of these proteins in virus-producing cells decreased the efficiency of viral entry and down-regulated HIV-1 envelope glycoproteins from the cell surface, resulting in reduced incorporation of envelope glycoproteins into virions, as observed in MARCH8 expression. With the demonstration that MARCH1 and MARCH2 are antiviral MARCH family members as presented here, these two proteins join a growing list of host factors that inhibit HIV-1 infection. Membrane-associated RING-CH 8 (MARCH8) is one of 11 members of the MARCH family of RING finger E3 ubiquitin ligases and down-regulates several membrane proteins (e.g. major histocompatibility complex II [MHC-II], CD86, and transferrin receptor). We recently reported that MARCH8 also targets HIV-1 envelope glycoproteins and acts as an antiviral factor. However, it remains unclear whether other family members might have antiviral functions similar to those of MARCH8. Here we show that MARCH1 and MARCH2 are MARCH family members that reduce virion incorporation of envelope glycoproteins. Infectivity assays revealed that MARCH1 and MARCH2 dose-dependently suppress viral infection. Treatment with type I interferon enhanced endogenous expression levels of MARCH1 and MARCH2 in monocyte-derived macrophages. Expression of these proteins in virus-producing cells decreased the efficiency of viral entry and down-regulated HIV-1 envelope glycoproteins from the cell surface, resulting in reduced incorporation of envelope glycoproteins into virions, as observed in MARCH8 expression. With the demonstration that MARCH1 and MARCH2 are antiviral MARCH family members as presented here, these two proteins join a growing list of host factors that inhibit HIV-1 infection. |
| Author | Yamaoka, Shoji Yao, Weitong Tada, Takuya Zhang, Yanzhao Kishigami, Satoshi Ozono, Seiya Tanaka, Michiko Fujita, Hideaki Tokunaga, Kenzo |
| Author_xml | – sequence: 1 givenname: Yanzhao surname: Zhang fullname: Zhang, Yanzhao organization: Department of Pathology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 2 givenname: Takuya surname: Tada fullname: Tada, Takuya organization: Department of Pathology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 3 givenname: Seiya surname: Ozono fullname: Ozono, Seiya organization: Department of Pathology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 4 givenname: Weitong surname: Yao fullname: Yao, Weitong organization: Department of Pathology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 5 givenname: Michiko surname: Tanaka fullname: Tanaka, Michiko organization: Department of Pathology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 6 givenname: Shoji surname: Yamaoka fullname: Yamaoka, Shoji organization: the Department of Molecular Virology, Tokyo Medical and Dental University, Tokyo 113-8519 – sequence: 7 givenname: Satoshi surname: Kishigami fullname: Kishigami, Satoshi organization: the Faculty of Life and Environmental Sciences, University of Yamanashi, Yamanashi 400-8510, Japan – sequence: 8 givenname: Hideaki surname: Fujita fullname: Fujita, Hideaki organization: the Faculty of Pharmaceutical Sciences, Nagasaki International University, Nagasaki 859-3298, Japan – sequence: 9 givenname: Kenzo orcidid: 0000-0002-2625-5322 surname: Tokunaga fullname: Tokunaga, Kenzo email: tokunaga@nih.go.jp organization: Department of Pathology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan |
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| Copyright | 2019 © 2019 Zhang et al. 2019 Zhang et al. 2019 Zhang et al. 2019 Zhang et al. |
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| Keywords | HIV-1 antiviral factor MARCH family HIV host–pathogen interaction membrane protein macrophage glycoprotein membrane-associated RING-CH |
| Language | English |
| License | This is an open access article under the CC BY license. 2019 Zhang et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc. |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Present address: Dept. of Microbiology, New York University School of Medicine, New York, New York. Both authors contributed equally to this work. Edited by Charles E. Samuel |
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| SubjectTerms | Amino Acid Sequence antiviral factor Carrier Proteins - chemistry Carrier Proteins - metabolism Cell Line glycoprotein HIV HIV-1 HIV-1 - physiology host–pathogen interaction Humans macrophage MARCH family membrane protein Membrane Proteins - chemistry Membrane Proteins - metabolism membrane-associated RING-CH Microbiology Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - metabolism |
| Title | Membrane-associated RING-CH (MARCH) 1 and 2 are MARCH family members that inhibit HIV-1 infection |
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