Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/23574
Title: Adverse reactions to vancomycin and cross-reactivity with other antibiotics.
Austin Authors: De Luca, Joseph F;Holmes, Natasha E ;Trubiano, Jason 
Affiliation: Department of Clinical Immunology and Allergy, The Royal Melbourne Hospital
The National Centre for Infections in Cancer, Peter MacCallum Cancer Centre, Melbourne, Victoria, Australia
Department of Infectious Diseases, Austin Health, Heidelberg, Victoria, Australia
Centre for Antibiotic Allergy and Research, Austin Health, Heidelberg, Victoria, Australia
Department of Medicine, Austin Health, The University of Melbourne, Heidelberg, Victoria, Australia
Issue Date: Aug-2020
Publication information: Current opinion in allergy and clinical immunology 2020; 20(4): 352-361
Abstract: Glycopeptide antibiotics such as vancomycin are frequently utilized to treat resistant Gram-positive infections such as methicillin-resistant Staphylococcus aureus. The current literature on glycopeptide and lipoglycopeptide structure, hypersensitivity and potential cross-reactivity was reviewed, highlighting implications for safe prescribing. Structurally similar, glycopeptides could theoretically cross-react. Immediate reactions to vancomycin include non-IgE-mediated reactions (e.g. red man syndrome) and IgE-mediated hypersensitivity (e.g. anaphylaxis), sharing clinical features. Vancomycin can activate mast cells via MAS-related G-protein-coupled receptor X2, an IgE-independent receptor implicated in non-IgE reactions. In-vivo and in-vitro testing for suspected IgE-mediated reactions to glycopeptides remain ill-defined. Vancomycin is increasingly recognized to cause severe cutaneous adverse reactions (SCAR), with drug reaction with eosinophilia and systemic symptoms (DRESS) predominantly reported. Vancomycin DRESS has been associated with HLA-A32:-01, with a number needed to prevent of 1 in 74. Data demonstrating cross-reactivity amongst glycopeptides and lipoglycopeptides is limited to case reports/series. Further studies and in-vivo/in-vitro diagnostics are required for better differentiation between IgE and non-IgE glycopeptide reactions. Despite its association with vanomycin DRESS, utility of pharmacogenomic screening for HLA-A32: 01 is ill-defined. Although HLA-A32:01 has been associated with vancomycin DRESS, its utility for pharmacogenomic screening is ill defined. Further clinical and immunological cross-reactivity data for glycopeptide/lipoglycopeptide antibiotics is required.
URI: https://ahro.austin.org.au/austinjspui/handle/1/23574
DOI: 10.1097/ACI.0000000000000665
ORCID: 0000-0001-8501-4054
0000-0002-5111-6367
Journal: Current opinion in allergy and clinical immunology
PubMed URL: 32590503
Type: Journal Article
Appears in Collections:Journal articles

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