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The provided name describes an immune response (a host immunological process) rather than a discrete molecular target such as a receptor, enzyme, transporter, or defined viral protein. In Lassa virus, the surface-exposed glycoprotein complex (GPC) is the trimeric spike that mediates entry and consists of glycoprotein 1 (GP1), glycoprotein 2 (GP2), and a stable signal peptide (SSP). GP1 binds host receptors—initially α-dystroglycan with matriglycan modifications at the cell surface and, after endocytosis and acidification, switches to LAMP1 in late endosomes—while GP2 executes pH-triggered membrane fusion; the SSP is retained as a third subunit unique to arenaviruses[2][4]. The GPC ectodomain is heavily N-glycosylated, forming a glycan shield (including a high-mannose cluster that spans GP1/GP2) that shapes antigenicity and partially occludes receptor-interaction sites until low pH conformational changes occur[3]. Neutralizing antibodies elicited by vaccination or infection can target conformational epitopes on GPC, with mapped competition groups (e.g., GPC-A, GPC-B, GPC-C, GP1-A) recognizing regions on GP1, GP2, or interfaces across protomers in the prefusion trimer; these antigenic insights are being used to design stabilized prefusion GPC immunogens for vaccines[5]. Given this, a correct therapeutic target entry would refer to the viral protein complex itself—Lassa virus glycoprotein complex (GPC)—or its subunits (GP1, GP2, SSP), not to the "adaptive immune response" to it[2][3][4][5].
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