The ADK1a antibody used for the AAV1 Titration ELISA as well as the ADK1b specifically recognize assembled AAV1 capsids, hence epitopes that result from a specific conformational assembly of the capsid proteins VP1, VP2 and VP3. In the publication cited below the contact sites and footprint residues identified for ADK1a and ADK1b are described and the results are summarized in table 1. Multiple contact sites and footprint residues have been identified, that are very likely to be part of the binding site. The amino acids of each binding site are located in different parts of the protein chains and are recognized as the epitope of the antibody only in the assembled capsid where they are in close proximity to each other and in the correct conformation.

For AAV1 the neutralization epitope has been identified and might give an additional indication about the binding residues of the neutralizing antibody ADK1 used for the corresponding AAV1 Titration ELISAs.

The A20 and A20R antibodies used for the AAV2 Titration ELISAs (PRATV & PRAAV2R) specifically recognize assembled AAV2 capsid, hence epitopes that result from a specific conformational assembly of the capsid proteins VP1, VP2 and VP3. Several publications cited below describe the analysis of binding sites for the A20 antibody using different techniques. Multiple amino acids have been identified, that are very likely to be part of the binding site, especially those that were identified with more than one method (green boxes). The amino acids of each binding site are located in different parts of the protein chains and are recognized as the epitope of the antibody only in the assembled capsid where they are in close proximity to each other and in the correct conformation.

The ADK5a  antibody used for the AAV5 Titration ELISA as well as the ADK5b specifically recognize assembled AAV5 capsids, hence epitopes that result from a specific conformational assembly of the capsid proteins VP1, VP2 and VP3. In the publication cited below the contact sites and footprint residues identified for ADK5a and ADK5b are described and the results are summarized in table 1. Multiple contact sites and footprint residues have been identified, that are very likely to be part of the binding site. The amino acids of each binding site are located in different parts of the protein chains and are recognized as the epitope of the antibody only in the assembled capsid where they are in close proximity to each other and in the correct conformation.

The ADK8 antibody used for the AAV8 Titration ELISA (PRAAV8) specifically recognizes assembled AAV8 capsid, hence epitopes that result from a specific conformational assembly of the capsid proteins VP1, VP2 and VP3. The publication cited below shows the result of the Cryo-EM analysis of binding sites for the ADK8 antibody. In this publication one potential epitope has been identified which is likely to be part of the ADK8 binding site.

For AAV9 the neutralization epitope has been identified and might give an additional indication about the binding residues of the neutralizing antibody ADK9 used for the corresponding AAV9 Titration ELISAs.

The ADK1a  antibody used for the AAV1 Titration ELISA as well as the ADK1b specifically recognize assembled AAV1 capsids, hence epitopes that result from a specific conformational assembly of the capsid proteins VP1, VP2 and VP3. In the publication cited below the contact sites and footprint residues identified for ADK1a and ADK1b are described and the results are summarized in table 1. Multiple contact sites and footprint residues have been identified, that are very likely to be part of the binding site. The amino acids of each binding site are located in different parts of the protein chains and are recognized as the epitope of the antibody only in the assembled capsid where they are in close proximity to each other and in the correct conformation.

For AAV1 the neutralization epitope has been identified and might give an additional indication about the binding residues of the neutralizing antibody ADK1 used for the corresponding AAV1 Titration ELISAs.

The A20 and A20R antibodies used for the AAV2 Titration ELISAs (PRATV & PRAAV2R) specifically recognize assembled AAV2 capsid, hence epitopes that result from a specific conformational assembly of the capsid proteins VP1, VP2 and VP3. Several publications cited below describe the analysis of binding sites for the A20 antibody using different techniques. Multiple amino acids have been identified, that are very likely to be part of the binding site, especially those that were identified with more than one method (green boxes). The amino acids of each binding site are located in different parts of the protein chains and are recognized as the epitope of the antibody only in the assembled capsid where they are in close proximity to each other and in the correct conformation.

The ADK5a  antibody used for the AAV5 Titration ELISA as well as the ADK5b specifically recognize assembled AAV5 capsids, hence epitopes that result from a specific conformational assembly of the capsid proteins VP1, VP2 and VP3. In the publication cited below the contact sites and footprint residues identified for ADK5a and ADK5b are described and the results are summarized in table 1. Multiple contact sites and footprint residues have been identified, that are very likely to be part of the binding site. The amino acids of each binding site are located in different parts of the protein chains and are recognized as the epitope of the antibody only in the assembled capsid where they are in close proximity to each other and in the correct conformation.

The ADK8 antibody used for the AAV8 Titration ELISA (PRAAV8) specifically recognizes assembled AAV8 capsid, hence epitopes that result from a specific conformational assembly of the capsid proteins VP1, VP2 and VP3. The publication cited below shows the result of the Cryo-EM analysis of binding sites for the ADK8 antibody. In this publication one potential epitope has been identified which is likely to be part of the ADK8 binding site.

For AAV9 the neutralization epitope has been identified and might give an additional indication about the binding residues of the neutralizing antibody ADK9 used for the corresponding AAV9 Titration ELISAs.