Extract-Shaped Immune Repertoires as Source for Nanobody-Based Human IgE in Grass Pollen Allergy

Aagaard, Josephine Baunvig; Fischer, Michaela; Lober, Julia; Neumann, Frederikke Bolbro; Allahverdi, Dena; Sivelle, Coline; Miehe, Michaela; Spillner, Edzard

doi:10.1007/s12033-023-00664-8

Cited by 5 publications

(2 citation statements)

References 41 publications

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“…Recently, smaller derivatives of antibodies with footprints of similar size have entered the stage in allergology. Nanobodies or single domain antibodies are the antigen-binding region in heavy chain only antibodies from camelid species (97). They comprise a single domain of 15 kDa with 3 CDRs only, involving predominantly the CDR3 for antigen interactions (98,99), which is on average longer than the CDR3 of conventional antibodies (98,100).…”

Section: Molecular Targeting Of Epitopes For Therapymentioning

confidence: 99%

“…In the context of allergic diseases, the use of blocking nanobodies for therapeutic purposes has been recently highlighted (101) and the generation of allergen-specific nanobodies has subsequently provided the initial corner stone for assessment of potential in allergy-related applications. Nanobodies have been generated against not only pollen allergens (97,102), and food allergens (103), but also venom allergens (104) and downstream formats like multimeric nanobodies and nanobody fusion proteins in the format of IgE have highlighted the ease of nanobody technologies.…”

Section: Molecular Targeting Of Epitopes For Therapymentioning

confidence: 99%

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Potential and limitations of epitope mapping and molecular targeting in Hymenoptera venom allergy

Fernandes,

Spillner,

Jakob

2023

Front. Allergy

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Hymenoptera venom (HV) allergy can lead to life threatening conditions by specific IgE (sIgE)-mediated anaphylactic reactions. The knowledge about major allergens from venom of different clinically relevant species increased in the last decades, allowing the development of component-resolved diagnostics in which sIgE to single allergens is analysed. Despite these advances, the precise regions of the allergens that bind to IgE are only known for few HV allergens. The detailed characterization of IgE epitopes may provide valuable information to improve immunodiagnostic tests and to develop new therapeutic strategies using allergen-derived peptides or other targeted approaches. Epitope-resolved analysis is challenging, since the identification of conformational epitopes present in many allergens demands complex technologies for molecular analyses. Furthermore, functional analysis of the epitopeś interaction with their respective ligands is needed to distinguish epitopes that can activate the allergic immune response, from those that are recognized by irrelevant antibodies or T cell receptors from non-effector cells. In this review, we focus on the use of mapping and molecular targeting approaches for characterization of the epitopes of the major venom allergens of clinically relevant Hymenoptera species. The screening of the most relevant allergen peptides by epitope mapping could be helpful for the development of molecules that target major and immunodominant epitopes blocking the allergen induced cellular reactions as novel approach for the treatment of HV allergy.

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