Virus neutralization (VN) responses range from narrowly focused antibodies with only homologous neutralizing activity against the virus used for infection, to antibodies that can neutralize both Type 1 and Type 2 viruses, referred to as broadly neutralizing antibody (bnAb). Even though neutralizing epitopes are likely distributed among several structural glycoproteins, this paper focuses on the ectodomain region of GP5 as a model system for investigating the role for neutralizing and non-neutralizing antibodies in protection and disease. Epitope B within GP5 possesses several features common to broadly neutralizing epitopes. In the proposed model, accessibility of antibody to Epitope B is blocked by homologous neutralizing and non-neutralizing antibodies, which bind flanking hypervariable domains. Additional mechanisms for blocking the accessibility of bnAb include conformational alterations within the GP5-M heterodimer and glycan shielding. This model explains how the continuous escape from homologous neutralization provides a mechanism for persistence. The proposed mechanism for immune evasion is not unique to PRRSV, but can be found in other persistent viruses, such as hepatitis C virus (HCV).
Keywords: Broadly neutralizing antibodies; HCV; Neutralizing epitopes; PRRS.
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