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Tailor made: New insights into lipoarabinomannan structure may improve TB diagnosis

Detecting the mycobacterial glycolipid lipoarabinomannan (LAM) in urine by anti-LAM antibodies fills a gap in the diagnostic armamentarium of much needed simple rapid tests for tuberculosis, but lacks high sensitivity in all patient groups. A better understanding of LAM structure from clinically rel...

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Detalles Bibliográficos
Autores principales: Lowary, Todd L., Achkar, Jacqueline M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8913296/
https://www.ncbi.nlm.nih.gov/pubmed/35122792
http://dx.doi.org/10.1016/j.jbc.2022.101678
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author Lowary, Todd L.
Achkar, Jacqueline M.
author_facet Lowary, Todd L.
Achkar, Jacqueline M.
author_sort Lowary, Todd L.
collection PubMed
description Detecting the mycobacterial glycolipid lipoarabinomannan (LAM) in urine by anti-LAM antibodies fills a gap in the diagnostic armamentarium of much needed simple rapid tests for tuberculosis, but lacks high sensitivity in all patient groups. A better understanding of LAM structure from clinically relevant strains may allow improvements in diagnostic performance. De et al. have recently determined the structures of LAM from three epidemiologically important lineages of Mycobacterium tuberculosis and probed their interaction with an anti-LAM monoclonal antibody. Their results not only identify a series of tailoring modifications that impact antibody binding but also provide a roadmap for improving U-LAM-based diagnostics.
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spelling pubmed-89132962022-03-18 Tailor made: New insights into lipoarabinomannan structure may improve TB diagnosis Lowary, Todd L. Achkar, Jacqueline M. J Biol Chem Editors' Pick Highlight Detecting the mycobacterial glycolipid lipoarabinomannan (LAM) in urine by anti-LAM antibodies fills a gap in the diagnostic armamentarium of much needed simple rapid tests for tuberculosis, but lacks high sensitivity in all patient groups. A better understanding of LAM structure from clinically relevant strains may allow improvements in diagnostic performance. De et al. have recently determined the structures of LAM from three epidemiologically important lineages of Mycobacterium tuberculosis and probed their interaction with an anti-LAM monoclonal antibody. Their results not only identify a series of tailoring modifications that impact antibody binding but also provide a roadmap for improving U-LAM-based diagnostics. American Society for Biochemistry and Molecular Biology 2022-02-02 /pmc/articles/PMC8913296/ /pubmed/35122792 http://dx.doi.org/10.1016/j.jbc.2022.101678 Text en © 2022 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Editors' Pick Highlight
Lowary, Todd L.
Achkar, Jacqueline M.
Tailor made: New insights into lipoarabinomannan structure may improve TB diagnosis
title Tailor made: New insights into lipoarabinomannan structure may improve TB diagnosis
title_full Tailor made: New insights into lipoarabinomannan structure may improve TB diagnosis
title_fullStr Tailor made: New insights into lipoarabinomannan structure may improve TB diagnosis
title_full_unstemmed Tailor made: New insights into lipoarabinomannan structure may improve TB diagnosis
title_short Tailor made: New insights into lipoarabinomannan structure may improve TB diagnosis
title_sort tailor made: new insights into lipoarabinomannan structure may improve tb diagnosis
topic Editors' Pick Highlight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8913296/
https://www.ncbi.nlm.nih.gov/pubmed/35122792
http://dx.doi.org/10.1016/j.jbc.2022.101678
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