Table 1.

An overview of the methods used and results generated in the six currently available published studies investigating phosphorylation in the mycobacteria using mass spectrometry.

References	Strain/species	Fractionation method	Enrichment method	# Proteins identified	# Sites	%S	%T	%Y	Major conclusions
Prisic et al., 2010	M. tuberculosis H37Rv	SDS PAGE	Titanium dioxide beads	301	516	40	60	-	A broad range of proteins are phosphorylated on S/T residues in M. tuberculosis, and may contribute to virulence.
Kusebauch et al., 2014	M. tuberculosis H37Rv	None	IMAC with PHOS-select iron affinity gel (Sigma) and then Titan-sphere Phos-TiO kit (GL Sciences Inc.)	232		32	64	4	Tyr phosphorylation does occur in M. tuberculosis, a Tyr phosphosite of PknB in is important in regulating growth and therefore may affect survival in stress conditions.
Parandhaman et al., 2014b	M. tuberculosis H37Rv, M. tuberculosisΔPknE mutant	2D SDS PAGE	None	68	N/A	N/A	N/A	N/A	Proteins which are affected by the ΔPknE mutation under NO stress are hypothesized to contribute to pathogenicity of M. tuberculosis.
Nakedi et al., 2015	M. bovis BCG	None	TiO2 beads	203	289	35	61.6	3.1	Differences between fast and slow growing mycobacteria may be related to phosphorylation, with the ability to respond rapidly to stress associated with metabolic cost and slow growth.
	M. smegmatis	None	TiO2 beads	76	106	39.47	57.02	3.51
Fortuin et al., 2015	M. tuberculosis clinical isolate	Strong cation exchange	TiO2 beads	214	414	38	59	3	Novel phosphorylation events were identified in this clinical strain, expanding our understanding of phosphorylation in M. tuberculosis.
Zheng et al., 2015	M. bovis BCG	SDS PAGE or offline ACN fractionation	TiO2 beads	398	659	39.5	48.7	11.8	Gel-based and gel-free phosphoproteomic analysis of M. tuberculosis may identify new pharmacological targets for drug development.