This study examines the mechanism utilized by different MARCH proteins to restrict retrovirus infection. MARCH proteins block the incorporation of envelope glycoproteins to the budding virions. ABSTRACT The membrane-associated RING-CH (MARCH) proteins belong to a family of E3 ubiquitin ligases, whose main function is to remove transmembrane proteins from the plasma membrane. Recent work has shown that the human MARCH1, 2, and 8 are antiretroviral factors that target the human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins by reducing their incorporation in the budding virions. Nevertheless, the dearth of information regarding the antiviral mechanism of this family of proteins necessitates further examination. In this study, using both the human MARCH proteins and their mouse homologues, we provide a comprehensive analysis of the antiretroviral mechanism of this family of proteins. Moreover, we show that human MARCH proteins restrict to various degrees the envelope glycoproteins of a diverse number of viruses. This report sheds light on the important antiviral function of MARCH proteins and their significance in cell intrinsic immunity.
【저자키워드】 Murine leukemia virus, Human immunodeficiency virus, retroviruses, host restriction factors, envelope glycoproteins, 【초록키워드】 viruses, Immunity, Antiviral, Infection, Proteins, Protein, HIV-1, glycoprotein, information, mechanism, Factor, comprehensive analysis, plasma membrane, virions, transmembrane protein, retrovirus, homologues, E3 ubiquitin ligases, antiretroviral, recent, Cell, intrinsic, shown, reducing, restrict, 【제목키워드】 Factor,