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Evidence for the presence of multiple neutralizing epitopes recognized by Abs in infected individuals is reviewed elsewhere [5].
It has been shown that the host cell surface receptor-binding motif of the E protein maps to EDIII [ 34]; further serotype-specific multiple neutralizing epitopes have been localized to this domain [ 35- 37].
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Recent studies have demonstrated that recombinant RBD consists of multiple conformational neutralizing epitopes that induce highly potent neutralizing antibodies against SARS-CoV (9, 26, 35– 35).
The spike (S) protein of SARS-CoV is the major inducer of neutralizing antibodies, and the receptor-binding domain (RBD) in the S1 subunit of S protein contains multiple conformational neutralizing epitopes.
The domain III of the dengue virus encoded envelope protein, which carries multiple conformation-dependent neutralizing epitopes, is critical for virus infectivity.
We previously demonstrated that the receptor-binding domain (RBD: residues 318 510) of S protein contains multiple conformation-dependent neutralizing epitopes (Conf I to VI) and serves as a major target of SARS-CoV neutralization.
To gain a better understanding of this, we will analyze (1) the neutralizing epitopes in MPER and neutralization mechanisms of MPER-specific bNAbs and (2) limitations in the elicitation of neutralizing antibodies.
However, the neutralizing epitopes of HEV are not completely defined.
This versatile ELISA targets well conformed neutralizing epitopes.
There exists marked shift in the predominant sequence patterns on these three neutralizing epitopes over time.
One approach is to design immunogens based on known broadly neutralizing epitopes.
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