Table 1.
Lipid posttranslational modifications (PTMs), hydrophobic membrane-spanning domains, sorting signals, and organellar localization of T. cruzi proteins extracted with Triton X-114 and identified by LC-MS/MS
| Lipid PTM, Hydrophobic Membrane-Spanning Domain, or Sorting Signal | Metacyclic Trypomastigote N (% total) a | Epimastigote N (% total) a |
|---|---|---|
| GPI Anchor | 21 (21.4%) | 1 (0.4%) |
| Myristoylation and Prenylation | 15 (15.3%) | 21 (7.5%) |
| Transmembrane Domain | 4 (4.1%) | 20 (7.1%) |
| Signal Peptide b | 26 (26.5%) | 72 (25.7%) |
|
Total |
66 (67.3%) |
114 (40.7%) |
|
Organelle distribution |
|
|
| Mitochondrial Targeting Sequence | 16 (16.3%) | 49 (17.5%) |
| Reservosomal membrane proteins | N/A c | 145 (51.8%) |
| Total d | 16 (16.3%) | 174 (62.1%) |
a
Number and percentage of the total identified proteins. Total proteins: metacyclic trypomastigotes, n=98 (100%); epimastigotes, n=280 (100%).
b
Proteins containing a typical ER signal peptide motif or an uncleaved signal-anchor sequence were included.
c
N/A, not applicable: reservosomes are not present in metacyclic trypomastigotes.60
d
Only non-redundant proteins.