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

Todd L. Lowary, Jacqueline M. Achkar

Research output: Contribution to journalComment/debatepeer-review

1 Scopus citations

Abstract

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.

Original languageEnglish (US)
Article number101678
JournalJournal of Biological Chemistry
Volume298
Issue number3
DOIs
StatePublished - Mar 2022

Keywords

  • acylation
  • lipoarabinomannan
  • monoclonal antibodies
  • mycobacteria
  • point-of-care diagnostics
  • polysaccharides
  • succinylation
  • tuberculosis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Tailor made: New insights into lipoarabinomannan structure may improve TB diagnosis'. Together they form a unique fingerprint.

Cite this