Expanding the Anti-Phl p 7 Antibody Toolkit: An Anti-Idiotype Nanobody Inhibitor

Vester, Susan K.; Davies, Anna M.; Beavil, Rebecca L.; Sandhar, Balraj S.; Beavil, Andrew J.; Gould, Hannah J.; Sutton, Brian J.; McDonnell, James M.

doi:10.3390/antib12040075

Cited by 3 publications

(1 citation statement)

References 43 publications

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“…Among some other published examples of the use of anti-idiotypic nanobodies, which are still rare but show great potential, ai-Nbs are usually produced against the idiotypes of classical antibodies [26][27][28][29][37][38][39]. We consider this an alternative possible route; however, in our experience, the efficiency of the generation and selection of ai-Nbs that mimic the epitope of the original target increases significantly if nanobodies are used as the primary idiotypes instead of mAbs.…”

Section: Discussionmentioning

confidence: 99%

Anti-Idiotypic Nanobodies Mimicking an Epitope of the Needle Protein of the Chlamydial Type III Secretion System for Targeted Immune Stimulation

Koroleva,

Goryainova,

Ivanova

et al. 2024

IJMS

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The development of new approaches and drugs for effective control of the chronic and complicated forms of urogenital chlamydia caused by Chlamydia trachomatis, which is suspected to be one of the main causes of infertility in both women and men, is an urgent task. We used the technology of single-domain antibody (nanobody) generation both for the production of targeting anti-chlamydia molecules and for the subsequent acquisition of anti-idiotypic nanobodies (ai-Nbs) mimicking the structure of a given epitope of the pathogen (the epitope of the Chlamydial Type III Secretion System Needle Protein). In a mouse model, we have shown that the obtained ai-Nbs are able to induce a narrowly specific humoral immune response in the host, leading to the generation of intrinsic anti-Chlamydia antibodies, potentially therapeutic, specifically recognizing a given antigenic epitope of Chlamydia. The immune sera derived from mice immunized with ai-Nbs are able to suppress chlamydial infection in vitro. We hypothesize that the proposed method of the creation and use of ai-Nbs, which mimic and present to the host immune system exactly the desired region of the antigen, create a fundamentally new universal approach to generating molecular structures as a part of specific vaccine for the targeted induction of immune response, especially useful in cases where it is difficult to prepare an antigen preserving the desired epitope in its native conformation.

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Section: Discussionmentioning

confidence: 99%

Anti-Idiotypic Nanobodies Mimicking an Epitope of the Needle Protein of the Chlamydial Type III Secretion System for Targeted Immune Stimulation

Koroleva,

Goryainova,

Ivanova

et al. 2024

IJMS

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The Crystal Structure of Human IgD‐Fc Reveals Unexpected Differences With Other Antibody Isotypes

Davies,

Bui,

Pacheco‐Gómez

et al. 2024

Proteins

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Of the five human antibody isotypes, the function of IgD is the least well‐understood, although various studies point to a role for IgD in mucosal immunity. IgD is also the least well structurally characterized isotype. Until recently, when crystal structures were reported for the IgD Fab, the only structural information available was a model for intact IgD based on solution scattering data. We now report the crystal structure of human IgD‐Fc solved at 3.0 Å resolution. Although similar in overall architecture to other human isotypes, IgD‐Fc displays markedly different orientations of the Cδ3 domains in the Cδ3 domain dimer and the lowest interface area of all the human isotypes. The nature of the residues that form the dimer interface also differs from those conserved in the other isotypes. By contrast, the interface between the Cδ2 and Cδ3 domains in each chain is the largest among the human isotypes. This interface is characterized by two binding pockets, not seen in other isotypes, and points to a potential role for the Cδ2/Cδ3 interface in stabilizing the IgD‐Fc homodimer. We investigated the thermal stability of IgD‐Fc, alone and in the context of an intact IgD antibody, and found that IgD‐Fc unfolds in a single transition. Human IgD‐Fc clearly has unique structural features not seen in the other human isotypes, and comparison with other mammalian IgD sequences suggests that these unique features might be widely conserved.

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Immune Jumping in Autoimmune Long-Covid

Kohler

2024

Monoclonal Antibodies in Immunodiagnosis and Immunotherapy

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Expanding the Anti-Phl p 7 Antibody Toolkit: An Anti-Idiotype Nanobody Inhibitor

Cited by 3 publications

References 43 publications

Anti-Idiotypic Nanobodies Mimicking an Epitope of the Needle Protein of the Chlamydial Type III Secretion System for Targeted Immune Stimulation

Anti-Idiotypic Nanobodies Mimicking an Epitope of the Needle Protein of the Chlamydial Type III Secretion System for Targeted Immune Stimulation

The Crystal Structure of Human IgD‐Fc Reveals Unexpected Differences With Other Antibody Isotypes

Immune Jumping in Autoimmune Long-Covid

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