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A Human Monoclonal Antibody Displays Promiscuous Binding to Multiple Type 1 nsLTP Allergens
Gage O Leighton1, Lars C Pedersen1, Jungki Min1
1Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, NIH, Durham, NC, USA.
Journal of Investigational Allergology & Clinical Immunology
|February 9, 2026
Summary
A novel human monoclonal antibody (mAb), IGX-3103, demonstrates cross-reactivity to multiple type 1 nonspecific lipid transfer proteins (nsLTPs). This finding suggests that a few promiscuous antibodies may drive widespread nsLTP cross-reactivity in allergies.
Area of Science:
- Allergen immunotherapy
- Immunology
- Structural biology
Background:
- Nonspecific lipid transfer proteins (nsLTPs) are common allergens causing cross-reactivity, complicating allergy diagnosis and avoidance strategies.
- Distinguishing true cross-reactivity from co-sensitization using polyclonal serum is challenging due to antibody complexity.
Purpose of the Study:
- To investigate if analyzing human monoclonal antibodies (mAbs) can differentiate cross-reactivity from co-sensitization.
- To characterize the binding properties and epitope of a specific mAb against nsLTPs.
Main Methods:
- Cloning and screening of human mAbs from allergic patients using single-cell sequencing.
- Expression and crystallization of Ara h 9 with mAb IGX-3103 for structural analysis.
- Affinity studies using molecular modeling, site-directed mutagenesis, and ELISA.
Main Results:
- A human IgG4 mAb, IGX-3103, was identified from a type 2-polarized memory B cell.
- IGX-3103 exhibited binding to 19 diverse type 1 nsLTP allergens and extracts.
- Structural analysis revealed IGX-3103 induces conformational changes in Ara h 9, allowing hydrophobic interactions within the lipid-binding cavity and identifying conserved epitope residues.
Conclusions:
- The human mAb IGX-3103 displays broad cross-reactivity against type 1 nsLTPs from various sources (pollen, fruit, seeds).
- This promiscuous binding supports the hypothesis that a limited number of specific mAbs can account for extensive cross-reactivity observed in nsLTP allergies.
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