TY - JOUR
T1 - The Mtb proteome library
T2 - A resource of assays to quantify the complete proteome of mycobacterium tuberculosis
AU - Schubert, Olga T.
AU - Mouritsen, Jeppe
AU - Ludwig, Christina
AU - Röst, Hannes L.
AU - Rosenberger, George
AU - Arthur, Patrick K.
AU - Claassen, Manfred
AU - Campbell, David S.
AU - Sun, Zhi
AU - Farrah, Terry
AU - Gengenbacher, Martin
AU - Maiolica, Alessio
AU - Kaufmann, Stefan H.E.
AU - Moritz, Robert L.
AU - Aebersold, Ruedi
PY - 2013/5/15
Y1 - 2013/5/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84877863368&partnerID=8YFLogxK
U2 - 10.1016/j.chom.2013.04.008
DO - 10.1016/j.chom.2013.04.008
M3 - Article
AN - SCOPUS:84877863368
SN - 1931-3128
VL - 13
SP - 602
EP - 612
JO - Cell Host and Microbe
JF - Cell Host and Microbe
IS - 5
ER -