Adeno-associated virus 2 capsid proteins and virus particles
Conjugate
Unconjugated
Applications
Application Notes
Suitable for use in ELISA, ICC/IF, IHC-Fr, IHC-P, IP, Neut. Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.
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Background
Adeno-associated viruses (AAV) are small, icosahedral viruses that have become one of the most important gene vectors in the field of gene therapy due to their long-term expression, low toxicity, low immunogenicity, and high tissue specificity. AAV2-based vectors are commonly used in gene therapy as they exhibit several desirable characteristics, including non-pathogenicity based on wild-type (wt) virus, the ability to infect dividing and non-dividing cells, and the establishment of long-term expression of heterologous genes by recombinant AAV. However, an important consideration in using this vector system is the high prevalence of anti-AAV-2 antibodies in humans. Many of these antibodies are neutralizing and may hinder the effectiveness of AAV2-based gene therapies. Several mechanisms of neutralization have been described, including interference with receptor attachment, inhibition of uncoating, induction of capsid structural changes, and interparticle cross-linking (aggregation). Identification of neutralizing epitopes can aid in the development of less immunogenic vectors. The anti-AAV2 (intact particle) monoclonal antibody (CABT-B9062) is a valuable tool for characterizing different stages of AAV2 infection and analyzing the AAV assembly process. It specifically targets intact AAV2 particles, including both empty and full capsids. One key feature of this monoclonal antibody is its recognition of a conformational epitope found on assembled capsids. This epitope is not present in denatured capsid proteins or native but unassembled capsid proteins. This means that the antibody selectively binds to AAV2 particles that have undergone the proper assembly process, providing a reliable marker for fully assembled and functional capsids. Moreover, the antibody's specificity for intact AAV2 particles makes it unsuitable for immunoblotting. This technique relies on the denaturation of proteins, which disrupts the conformational epitopes recognized by the Anti-AAV2 (intact particle) monoclonal antibody. Therefore, alternative methods such as immunofluorescence or ELISA are more appropriate for the detection and analysis of intact AAV2 particles using this antibody.
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References
Anti-AAV Antibodies in AAV Gene Therapy: Current Challenges and Possible Solutions
Adeno-associated virus (AAV) vector-based gene therapy is currently the only in vivo gene therapy approved in the US and Europe. The recent tragic death of three children in a clinical trial to treat X-Linked Myotubular Myopathy by delivering myotubularin with an AAV8 vector notwithstanding, AAV remains a highly promising therapeutic gene delivery platform. But the successful use of AAV vectors to treat an increasing number of diseases also makes establishing protocols to determine therapeutically relevant titers of pre-existing anti-AAV antibodies and approaches to deplete those antibodies more urgent than ever. In this mini review, I will briefly discuss (i) our knowledge regarding the prevalence of anti-AAV antibodies, (ii) the challenges to measure those antibodies by methods that are most predictive of their influence on therapeutic efficacy of AAV gene transfer, and (iii) approaches to overcome the formidable hurdle that anti-AAV antibodies pose to the successful clinical use of AAV gene therapy.
Monoclonal Antibodies against the Adeno-Associated Virus Type 2 (AAV-2) Capsid: Epitope Mapping and Identification of Capsid Domains Involved in AAV-2–Cell Interaction and Neutralization of AAV-2 Infection
Journal of Virology
Authors: Wobus C E, Hügle-Dörr B, Girod A, et al.
The previously characterized monoclonal antibodies (MAbs) A1, A69, B1, and A20 are directed against assembled or nonassembled adeno-associated virus type 2 (AAV-2) capsid proteins (A. Wistuba, A. Kern, S. Weger, D. Grimm, and J. A. Kleinschmidt, J. Virol. 71:1341–1352, 1997). Here we describe the linear epitopes of A1, A69, and B1 which reside in VP1, VP2, and VP3, respectively, using gene fragment phage display library, peptide scan, and peptide competition experiments. In addition, MAbs A20, C24-B, C37-B, and D3 directed against conformational epitopes on AAV-2 capsids were characterized. Epitope sequences on the capsid surface were identified by enzyme-linked immunoabsorbent assay using AAV-2 mutants and AAV serotypes, peptide scan, and peptide competition experiments. A20 neutralizes infection following receptor attachment by binding an epitope formed during AAV-2 capsid assembly. The newly isolated antibodies C24-B and C37-B inhibit AAV-2 binding to cells, probably by recognizing a loop region involved in binding of AAV-2 to the cellular receptor. In contrast, binding of D3 to a loop near the predicted threefold spike does not neutralize AAV-2 infection. The identified antigenic regions on the AAV-2 capsid surface are discussed with respect to their possible roles in different steps of the viral life cycle.
COA
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