The influence of the carrier molecule on amoxicillin recognition by specific IgE in patients with immediate hypersensitivity reactions to betalactams.

The optimal recognition of penicillin determinants, including amoxicillin (AX), by specific IgE antibodies is widely believed to require covalent binding to a carrier molecule. The nature of the carrier and its contribution to the antigenic determinant is not well known. Here we aimed to evaluate th...

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Detalles Bibliográficos
Autores: Ariza, Adriana, Mayorga, Cristobalina, Salas, María, Doña, Inmaculada, Martín-Serrano, Ángela, Pérez-Inestrosa, Ezequiel, Pérez-Sala, Dolores, Guzmán, Antonio E, Montañez, María I, Torres, María J
Tipo de recurso: artículo
Fecha de publicación:2016
País:España
Institución:Instituto de Salud Carlos III (ISCIII)
Repositorio:Repisalud
Idioma:inglés
OAI Identifier:oai:repisalud.isciii.es:20.500.12105/17163
Acceso en línea:http://hdl.handle.net/20.500.12105/17163
Access Level:acceso abierto
Palabra clave:Adult
Aged
Amoxicillin
Anaphylaxis
Antibody Specificity
Butylamines
Carrier Proteins
Cross Reactions
Drug Hypersensitivity
Female
Haptens
Humans
Hypersensitivity, Immediate
Immunoglobulin E
Male
Middle Aged
Penicillins
Polylysine
Serum Albumin, Human
Urticaria
Young Adult
beta-Lactams
Descripción
Sumario:The optimal recognition of penicillin determinants, including amoxicillin (AX), by specific IgE antibodies is widely believed to require covalent binding to a carrier molecule. The nature of the carrier and its contribution to the antigenic determinant is not well known. Here we aimed to evaluate the specific-IgE recognition of different AX-derived structures. We studied patients with immediate hypersensitivity reactions to AX, classified as selective or cross-reactors to penicillins. Competitive immunoassays were performed using AX itself, amoxicilloic acid, AX bound to butylamine (AXO-BA) or to human serum albumin (AXO-HSA) in the fluid phase, as inhibitors, and amoxicilloyl-poli-L-lysine (AXO-PLL) in the solid-phase. Two distinct patterns of AX recognition by IgE were found: Group A showed a higher recognition of AX itself and AX-modified components of low molecular weights, whilst Group B showed similar recognition of both unconjugated and conjugated AX. Amoxicilloic acid was poorly recognized in both groups, which reinforces the need for AX conjugation to a carrier for optimal recognition. Remarkably, IgE recognition in Group A (selective responders to AX) is influenced by the mode of binding and/or the nature of the carrier; whereas IgE in Group B (cross-responders to penicillins) recognizes AX independently of the nature of the carrier.