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Viral infection-associated antigens are virus-encoded proteins or glycoproteins expressed on the plasma membrane of host cells during an active infection. These antigens, such as the HIV-1 envelope glycoprotein (Env), Hepatitis B surface antigen (HBsAg), or the SARS-CoV-2 Spike protein, are essential for viral processes including attachment, fusion, and the budding of new progeny (PMID: 32855319, PMID: 29449661). Because they are uniquely present on infected cells, they serve as primary targets for the host's immune system and for various therapeutic modalities, including monoclonal antibodies and chimeric antigen receptor (CAR) T-cells (PMID: 31620131). Therapeutic strategies often aim to neutralize free virus and trigger effector mechanisms like antibody-dependent cellular cytotoxicity (ADCC) to eliminate the infected cell reservoir (Janeway's Immunobiology, 9th Ed). However, the effectiveness of targeting these antigens is frequently challenged by high viral mutation rates, which lead to antigenic drift and immune escape (PMID: 28619717). Furthermore, some viruses can establish latency, where they reside within the host cell without expressing these surface antigens, thereby evading detection and complicating eradication efforts (Nature Reviews Drug Discovery, 2018). Despite these challenges, viral surface antigens remain a cornerstone of vaccine design and antiviral immunotherapy development.
Neutralization of viral entry, induction of antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), complement-dependent cytotoxicity (CDC), and direct T-cell mediated lysis of infected cells.
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