Assessment of Antipiperacillin IgG Binding to Structurally Related Drug Protein Adducts



Amali, Mohammed O, Jenkins, Rosalind E, Meng, Xiaoli ORCID: 0000-0002-7774-2075, Faulkner, Lee, Whitaker, Paul, Peckham, Daniel, Park, B Kevin ORCID: 0000-0001-8384-824X and Naisbitt, Dean J
(2017) Assessment of Antipiperacillin IgG Binding to Structurally Related Drug Protein Adducts. CHEMICAL RESEARCH IN TOXICOLOGY, 30 (12). pp. 2097-2099.

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Abstract

The risk of developing hypersensitivity to alternative antibiotics is a concern for penicillin hypersensitive patients and healthcare providers. Herein we use piperacillin hypersensitivity as a model to explore the reactivity of drug-specific IgG against alternative β-lactam protein adducts. Mass spectrometry was used to show the drugs (amoxicillin, flucloxacillin, benzyl penicillin, aztreonam, and piperacillin) bind to similar lysine residues on the protein carrier bovine serum albumin. However, the hapten-specific IgG antibodies found in piperacillin hypersensitive patient plasma did not bind to other β-lactam protein conjugates. These data outline the fine specificity of piperacillin-specific IgG antibodies that circulate in patients with hypersensitivity.

Item Type: Article
Uncontrolled Keywords: Humans, Drug Hypersensitivity, beta-Lactams, Piperacillin, Immunoglobulin G, Anti-Bacterial Agents, Protein Binding
Depositing User: Symplectic Admin
Date Deposited: 01 Dec 2017 16:03
Last Modified: 19 Jan 2023 06:48
DOI: 10.1021/acs.chemrestox.7b00291
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3013302