The Mtb proteome library: A resource of assays to quantify the complete proteome of mycobacterium tuberculosis

Olga T. Schubert, Jeppe Mouritsen, Christina Ludwig, Hannes L. Röst, George Rosenberger, Patrick K. Arthur, Manfred Claassen, David S. Campbell, Zhi Sun, Terry Farrah, Martin Gengenbacher, Alessio Maiolica, Stefan H.E. Kaufmann, Robert L. Moritz, Ruedi Aebersold

Research output: Contribution to journalArticlepeer-review

150 Citations (Scopus)

Abstract

Research advancing our understanding of Mycobacterium tuberculosis (Mtb) biology and complex host-Mtb interactions requires consistent and precise quantitative measurements of Mtb proteins. We describe the generation and validation of a compendium of assays to quantify 97% of the 4,012 annotated Mtb proteins by the targeted mass spectrometric method selected reaction monitoring (SRM). Furthermore, we estimate the absolute abundance for 55% of all Mtb proteins, revealing a dynamic range within the Mtb proteome of over four orders of magnitude, and identify previously unannotated proteins. As an example of the assay library utility, we monitored the entire Mtb dormancy survival regulon (DosR), which is linked to anaerobic survival and Mtb persistence, and show its dynamic protein-level regulation during hypoxia. In conclusion, we present a publicly available research resource that supports the sensitive, precise, and reproducible quantification of virtually any Mtb protein by a robust and widely accessible mass spectrometric method.

Original languageEnglish
Pages (from-to)602-612
Number of pages11
JournalCell Host and Microbe
Volume13
Issue number5
DOIs
Publication statusPublished - 15 May 2013

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