Why the study?
Neutralizing antibodies prevent PCV2-associated diseases, and although MAb 3A5 neutralizes PCV2a, PCV2b, and PCV2d genotypes with differing efficiency, the underlying mechanism was unknown.
The structural elucidation of the PCV2 virion in complex with MAb 3A5 provides novel insights into the neutralization mechanism, informing future vaccine design and therapeutic antibody development against PCV2.
Elucidates MAb 3A5 neutralization mechanism across PCV2 genotypes; extends structural insights but leaves clinical translation open.
PCV2 is associated with several clinical manifestations collectively known as PCV2-associated diseases (PCVADs). Neutralizing antibodies play a crucial role in the prevention of PCVADs. We demonstrated previously that a MAb, MAb 3A5, neutralizes the PCV2a, PCV2b, and PCV2d genotypes with different degrees of efficiency, but the underlying mechanism remains elusive. Here, we report the neutralization mechanism of this MAb and the structure of the PCV2 virion in complex with MAb 3A5 Fabs, showing a binding mode in which one Fab interacted with more than two loops from two adjacent capsid proteins. This binding mode has not been observed previously for PCV2-neutralizing antibodies. Our work provides new and important information for vaccine design and therapeutic antibody development against PCV2 infections.
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Huang et al. (2020) studied this question.
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