Identification of Unambiguous Borrelia Peptides in Human Urine Using Affinity Capture and Mass Spectrometry

Rocio Cornero; Sumaiya Safia Irfan; Silvia Cachaco; Weidong Zhou; Ahana Byne; Marissa Howard; Hope McIntyre; Barbara Birkaya; Lance Liotta; Alessandra Luchini

doi:10.1007/978-1-0716-3561-2_9

Identification of Unambiguous Borrelia Peptides in Human Urine Using Affinity Capture and Mass Spectrometry

Methods Mol Biol. 2024:2742:105-122. doi: 10.1007/978-1-0716-3561-2_9.

Affiliations

¹ Center for Applied Proteomics and Molecular Medicine, George Mason University, Manassas, VA, USA.
² Lyme Hope, LLC, Mount Airy, MD, USA.
³ Center for Applied Proteomics and Molecular Medicine, George Mason University, Manassas, VA, USA. aluchini@gmu.edu.

PMID: 38165619
DOI: 10.1007/978-1-0716-3561-2_9

Abstract

The combination of advanced mass spectrometry and enrichment-based sample preparation methods has enhanced analytical capabilities in clinical proteomics. In this chapter, we describe a method of proteome analysis to identify Borrelia-derived peptides in urine that includes a sample affinity enrichment method coupled with liquid chromatography tandem mass spectrometry analysis and a bioinformatic peptide authentication algorithm.

Keywords: Affinity capture; Borrelia; Direct test; Mass spectrometry; Polyamide; Sudan IV; Sudan black B; Urine.

MeSH terms

Borrelia*
Chromatography, Liquid / methods
Humans
Peptides / chemistry
Proteome / analysis
Tandem Mass Spectrometry / methods

Substances

Peptides
Proteome