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Deemah Dabbagh
National Center for Biodefense and Infectious Diseases, School of Systems Biology, George Mason University, Manassas, VA 20110, USA

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Journal article
Published: 04 May 2021 in Viruses
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Mucins and mucin-like molecules are highly glycosylated, high-molecular-weight cell surface proteins that possess a semi-rigid and highly extended extracellular domain. P-selectin glycoprotein ligand-1 (PSGL-1), a mucin-like glycoprotein, has recently been found to restrict HIV-1 infectivity through virion incorporation that sterically hinders virus particle attachment to target cells. Here, we report the identification of a family of antiviral cellular proteins, named the Surface-Hinged, Rigidly-Extended Killer (SHREK) family of virion inactivators (PSGL-1, CD43, TIM-1, CD34, PODXL1, PODXL2, CD164, MUC1, MUC4, and TMEM123) that share similar structural characteristics with PSGL-1. We demonstrate that SHREK proteins block HIV-1 infectivity by inhibiting virus particle attachment to target cells. In addition, we demonstrate that SHREK proteins are broad-spectrum host antiviral factors that block the infection of diverse viruses such as influenza A. Furthermore, we demonstrate that a subset of SHREKs also blocks the infectivity of a hybrid alphavirus-SARS-CoV-2 (Ha-CoV-2) pseudovirus. These results suggest that SHREK proteins may be a part of host innate immunity against enveloped viruses.

ACS Style

Deemah Dabbagh; Sijia He; Brian Hetrick; Linda Chilin; Ali Andalibi; Yuntao Wu. Identification of the SHREK Family of Proteins as Broad-Spectrum Host Antiviral Factors. Viruses 2021, 13, 832 .

AMA Style

Deemah Dabbagh, Sijia He, Brian Hetrick, Linda Chilin, Ali Andalibi, Yuntao Wu. Identification of the SHREK Family of Proteins as Broad-Spectrum Host Antiviral Factors. Viruses. 2021; 13 (5):832.

Chicago/Turabian Style

Deemah Dabbagh; Sijia He; Brian Hetrick; Linda Chilin; Ali Andalibi; Yuntao Wu. 2021. "Identification of the SHREK Family of Proteins as Broad-Spectrum Host Antiviral Factors." Viruses 13, no. 5: 832.

Brief report
Published: 30 December 2020 in Viruses
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P-selectin glycoprotein ligand-1 (PSGL-1) is a cell surface glycoprotein that binds to P-, E-, and L-selectins to mediate the tethering and rolling of immune cells on the surface of the endothelium for cell migration into inflamed tissues. PSGL-1 has been identified as an interferon-γ (INF-γ)-regulated factor that restricts HIV-1 infectivity, and has recently been found to possess broad-spectrum antiviral activities. Here we report that the expression of PSGL-1 in virus-producing cells impairs the incorporation of SARS-CoV and SARS-CoV-2 spike (S) glycoproteins into pseudovirions and blocks pseudovirus attachment and infection of target cells. These findings suggest that PSGL-1 may potentially inhibit coronavirus replication in PSGL-1+ cells

ACS Style

Sijia He; Abdul A. Waheed; Brian Hetrick; Deemah Dabbagh; Ivan V. Akhrymuk; Kylene Kehn-Hall; Eric O. Freed; Yuntao Wu. PSGL-1 Inhibits the Incorporation of SARS-CoV and SARS-CoV-2 Spike Glycoproteins into Pseudovirions and Impairs Pseudovirus Attachment and Infectivity. Viruses 2020, 13, 46 .

AMA Style

Sijia He, Abdul A. Waheed, Brian Hetrick, Deemah Dabbagh, Ivan V. Akhrymuk, Kylene Kehn-Hall, Eric O. Freed, Yuntao Wu. PSGL-1 Inhibits the Incorporation of SARS-CoV and SARS-CoV-2 Spike Glycoproteins into Pseudovirions and Impairs Pseudovirus Attachment and Infectivity. Viruses. 2020; 13 (1):46.

Chicago/Turabian Style

Sijia He; Abdul A. Waheed; Brian Hetrick; Deemah Dabbagh; Ivan V. Akhrymuk; Kylene Kehn-Hall; Eric O. Freed; Yuntao Wu. 2020. "PSGL-1 Inhibits the Incorporation of SARS-CoV and SARS-CoV-2 Spike Glycoproteins into Pseudovirions and Impairs Pseudovirus Attachment and Infectivity." Viruses 13, no. 1: 46.

Preprint content
Published: 02 May 2020
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P-selectin glycoprotein ligand-1 (PSGL-1) is a cell surface glycoprotein that binds to P-, E-, and L-selectins to mediate the tethering and rolling of immune cells on the surface of the endothelium for cell migration into inflamed tissues. PSGL-1 has been identified as an interferon-γ (INF-γ)-regulated factor that restricts HIV-1 infectivity, and has recently been found to possess broad-spectrum antiviral activities. Here we report that the expression of PSGL-1 in virus-producing cells impairs the incorporation of SARS-CoV and SARS-CoV-2 spike (S) glycoproteins into pseudovirions and blocks virus attachment and infection of target cells. These findings suggest that PSGL-1 may potentially inhibit coronavirus replication in PSGL-1+ cells.

ACS Style

Sijia He; Abdul A. Waheed; Brian Hetrick; Deemah Dabbagh; Ivan V. Akhrymuk; Kylene Kehn-Hall; Eric O. Freed; Yuntao Wu. PSGL-1 inhibits the virion incorporation of SARS-CoV and SARS-CoV-2 spike glycoproteins and impairs virus attachment and infectivity. 2020, 1 .

AMA Style

Sijia He, Abdul A. Waheed, Brian Hetrick, Deemah Dabbagh, Ivan V. Akhrymuk, Kylene Kehn-Hall, Eric O. Freed, Yuntao Wu. PSGL-1 inhibits the virion incorporation of SARS-CoV and SARS-CoV-2 spike glycoproteins and impairs virus attachment and infectivity. . 2020; ():1.

Chicago/Turabian Style

Sijia He; Abdul A. Waheed; Brian Hetrick; Deemah Dabbagh; Ivan V. Akhrymuk; Kylene Kehn-Hall; Eric O. Freed; Yuntao Wu. 2020. "PSGL-1 inhibits the virion incorporation of SARS-CoV and SARS-CoV-2 spike glycoproteins and impairs virus attachment and infectivity." , no. : 1.

Abstract
Published: 01 January 2020 in Proceedings
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P-selectin glycoprotein ligand-1 (PSGL-1) is a dimeric, mucin-like, 120-kDa glycoprotein that binds to P-, E-, and L-selectins. PSGL-1 is primarily expressed on the surface of lymphoid and myeloid cells and is up-regulated during inflammation to mediate leukocyte tethering and rolling on the surface of endothelium for migration into inflamed tissues. Although it has been reported that PSGL-1 expression inhibits human immunodeficiency virus type 1 (HIV-1) replication, the mechanism of PSGL-1-mediated anti-HIV activity remains to be elucidated. Here, we report that PSGL-1 in virions blocks the infectivity of HIV-1 particles by preventing the binding of particles to target cells. This inhibitory activity is independent of the viral glycoprotein present on the virus particle; the binding of particles bearing the HIV-1 envelope glycoprotein, vesicular stomatitis virus G glycoprotein, or lacking a viral glycoprotein, is impaired by PSGL-1. Mapping studies show that the extracellular, N-terminal domain of PSGL-1 is necessary for its anti-HIV-1 activity, and the PSGL-1 cytoplasmic tail contributes to its inhibition. In addition, we demonstrate that the PSGL-1-related monomeric E-selectin-binding glycoprotein CD43 also effectively blocks HIV-1 infectivity. HIV-1 infection, or the expression of either Vpu or Nef, downregulates PSGL-1 from the cell surface; the expression of Vpu appears to be primarily responsible for enabling the virus to partially escape PSGL-1-mediated restriction. Finally, we show that PSGL-1 inhibits the infectivity of other viruses such as murine leukemia virus and influenza A virus. These findings demonstrate that PSGL-1 is a broad-spectrum antiviral host factor with a novel mechanism of action.

ACS Style

Yajing Fu; Sijia He; Abdul Waheed; Deemah Dabbagh; Zheng Zhou; Benjamin Trinité; Zhao Wang; Jieshi Yu; Dan Wang; Feng Li; David N Levy; Hong Shang; Eric O Freed; Yuntao Wu. PSGL-1 Restricts HIV-1 Infectivity by Blocking Virus Particle Attachment to Target Cells. Proceedings 2020, 50, 77 .

AMA Style

Yajing Fu, Sijia He, Abdul Waheed, Deemah Dabbagh, Zheng Zhou, Benjamin Trinité, Zhao Wang, Jieshi Yu, Dan Wang, Feng Li, David N Levy, Hong Shang, Eric O Freed, Yuntao Wu. PSGL-1 Restricts HIV-1 Infectivity by Blocking Virus Particle Attachment to Target Cells. Proceedings. 2020; 50 (1):77.

Chicago/Turabian Style

Yajing Fu; Sijia He; Abdul Waheed; Deemah Dabbagh; Zheng Zhou; Benjamin Trinité; Zhao Wang; Jieshi Yu; Dan Wang; Feng Li; David N Levy; Hong Shang; Eric O Freed; Yuntao Wu. 2020. "PSGL-1 Restricts HIV-1 Infectivity by Blocking Virus Particle Attachment to Target Cells." Proceedings 50, no. 1: 77.