MARCH2 (Membrane-Associated RING-CH 2) is an E3 ubiquitin ligase belonging to the MARCH protein family, which regulates cell-surface protein turnover through ubiquitination . It plays a critical role in antiviral immunity, particularly against HIV-1, by restricting viral envelope glycoprotein incorporation into nascent virions and inhibiting viral entry . Human MARCH2 exhibits distinct antiviral properties compared to its murine ortholog due to evolutionary adaptations, such as the presence of Gly61, a residue critical for its HIV-1 restriction function .
The MARCH2 Antibody (NBP1-60051) from Bio-Techne is a polyclonal rabbit IgG antibody designed for detecting human MARCH2 in Western blot applications .
MARCH2 inhibits HIV-1 through two distinct mechanisms:
RING-CH-Dependent Envelope Exclusion: Reduces HIV-1 Env (gp120/gp41) incorporation into virions by ubiquitinating viral glycoproteins .
RING-CH-Independent Fusion Blockade: Incorporated into virions to disrupt virus-cell membrane fusion during entry .
MARCH2 restricts HIV-1 replication exclusively in CD4+ T cells, with no effect in monocyte-derived macrophages (MDMs) . It reduces cell-to-cell transmission by 5-fold in primary T cells .
HIV-1 Restriction Studies: Used to quantify MARCH2-mediated Env depletion in virions and assess its role in viral fusion .
Protein Localization: Identifies MARCH2’s subcellular redistribution during HIV-1 infection, including plasma membrane co-localization with viral Gag .
Functional Knockdown: Validates endogenous MARCH2’s role in primary T cells using shRNA-depletion models .