SARS1抗体;SARS1 Antibody—艾普蒂

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane: Human fetal brain tissue lysate, Primary antibody: P10192(SARS1 Antibody) at dilution 1/850, Secondary antibody: Goat anti rabbit IgG at 1/5000 dilution, Exposure time: 40 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P10192(SARS1 Antibody) at dilution 1/65. (Original magnification: ×200)    

  
  

SARS-CoV-1 antibodies emerged following the 2002-2003 outbreak of severe acute respiratory syndrome (SARS) caused by the SARS-CoV-1 coronavirus. These antibodies are immune proteins produced by B cells, primarily targeting the viral spike (S) glycoprotein, which mediates host cell entry by binding to angiotensin-converting enzyme 2 (ACE2) receptors. Neutralizing antibodies block this interaction, preventing viral infection. Studies identified both IgM (early response) and IgG (long-term immunity) antibodies, with IgG persisting for years in recovered patients, though titers gradually decline.

Research revealed that SARS-CoV-1 antibodies exhibit cross-reactivity with other coronaviruses, including SARS-CoV-2. due to conserved regions in the S protein. However, antibody-dependent enhancement (ADE) of infection was a concern, as some subneutralizing antibodies were shown to facilitate viral entry into immune cells in vitro, though clinical relevance remains unclear. Monoclonal antibodies (mAbs) like CR3022. isolated from convalescent patients, demonstrated potent neutralization and informed therapeutic development. Structural studies mapped epitopes to the receptor-binding domain (RBD) and other S protein regions, guiding vaccine design.

SARS-CoV-1 antibody research laid groundwork for COVID-19 responses, highlighting the importance of neutralizing epitopes, immune memory, and potential risks like ADE. These insights remain critical for pandemic preparedness against novel coronaviruses.