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Giardia lamblia and trichomonas vaginalis flagella proteomic analysis

Maria Reed

Microtubules make up all eukaryotic flagella, which are propelled by dynein motor proteins. Every organism, on the other hand, has its own flagellar waveform, beat frequency, and general motility pattern. Recent research has revealed that, despite overall flagellar structure conservation, the distribution of tubulin post-translational modifications inside the flagella is different, which may contribute to variances in motility patterns. Using global, untargeted mass spectrometry, we investigated tubulin post-translational modification in the protozoan parasites Giardia lamblia and Trichomonas vaginalis. We show that tubulin monoglycylation is a flagellaspecific alteration found in G. lamblia but not in T. vaginalis. We also discovered glutamylated tubulin in both G. lamblia and T. vaginalis. We were also able to locate previously unknown monoglycylation sites in -tubulin at E438 and E439 in G. lamblia using MS/MS. We analysed the flagellar proteome in G. lamblia and T. vaginalis flagella using isolated flagella and found 475 proteins in G. lamblia flagella and 386 proteins in T. vaginalis flagella. Overall, the flagellar proteomes and tubulin PTM sites in these species show potential mechanisms for regulating flagellar motility in these understudied protozoan parasites.