@article{WeisseHeddergottHeydtetal.2012,
  author    = {Weiße, Sebastian and Heddergott, Niko and Heydt, Matthias and Pfl{\"a}sterer, Daniel and Maier, Timo and Haraszti, Tamas and Grunze, Michael and Engstler, Markus and Rosenhahn, Axel},
  title     = {A Quantitative 3D Motility Analysis of Trypanosoma brucei by Use of Digital In-line Holographic Microscopy},
  series = {PLoS One},
  volume    = {7},
  journal   = {PLoS One},
  number    = {5},
  doi       = {10.1371/journal.pone.0037296},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-130666},
  pages     = {e37296},
  year      = {2012},
  abstract  = {We present a quantitative 3D analysis of the motility of the blood parasite Trypanosoma brucei. Digital in-line holographic microscopy has been used to track single cells with high temporal and spatial accuracy to obtain quantitative data on their behavior. Comparing bloodstream form and insect form trypanosomes as well as mutant and wildtype cells under varying external conditions we were able to derive a general two-state-run-and-tumble-model for trypanosome motility. Differences in the motility of distinct strains indicate that adaption of the trypanosomes to their natural environments involves a change in their mode of swimming.},
  language  = {en}
}
@article{TalmanPrietoMarquesetal.2014,
  author    = {Talman, Arthur M. and Prieto, Judith H. and Marques, Sara and Ubaida-Mohien, Ceereena and Lawniczak, Mara and Wass, Mark N. and Xu, Tao and Frank, Roland and Ecker, Andrea and Stanway, Rebecca S. and Krishna, Sanjeev and Sternberg, Michael J. E. and Christophides, Georges K. and Graham, David R. and Dinglasan, Rhoel R. and Yates, John R., III and Sinden, Robert E.},
  title     = {Proteomic analysis of the Plasmodium male gamete reveals the key role for glycolysis in flagellar motility},
  series = {Malaria Journal},
  volume    = {13},
  journal   = {Malaria Journal},
  number    = {315},
  doi       = {10.1186/1475-2875-13-315},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-115572},
  year      = {2014},
  abstract  = {Background: Gametogenesis and fertilization play crucial roles in malaria transmission. While male gametes are thought to be amongst the simplest eukaryotic cells and are proven targets of transmission blocking immunity, little is known about their molecular organization. For example, the pathway of energy metabolism that power motility, a feature that facilitates gamete encounter and fertilization, is unknown. Methods: Plasmodium berghei microgametes were purified and analysed by whole-cell proteomic analysis for the first time. Data are available via ProteomeXchange with identifier PXD001163. Results: 615 proteins were recovered, they included all male gamete proteins described thus far. Amongst them were the 11 enzymes of the glycolytic pathway. The hexose transporter was localized to the gamete plasma membrane and it was shown that microgamete motility can be suppressed effectively by inhibitors of this transporter and of the glycolytic pathway. Conclusions: This study describes the first whole-cell proteomic analysis of the malaria male gamete. It identifies glycolysis as the likely exclusive source of energy for flagellar beat, and provides new insights in original features of Plasmodium flagellar organization.},
  language  = {en}
}
@phdthesis{Cicova2016,
  author    = {Cicova, Zdenka},
  title     = {Characterization of a novel putative factor involved in host adaptation in Trypanosoma brucei},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-142462},
  school      = {Universit{\"a}t W{\"u}rzburg},
  year      = {2016},
  abstract  = {Trypanosomes are masters of adaptation to different host environments during their complex life cycle. Large-scale proteomic approaches provide information on changes at the cellular level in a systematic way. However, a detailed work on single components is necessary to understand the adaptation mechanisms on a molecular level. Here we have performed a detailed characterization of a bloodstream form (BSF) stage-specific putative flagellar host adaptation factor (Tb927.11.2400) identified previously in a SILAC-based comparative proteome study. Tb927.11.2400 shares 38\% amino acid identity with TbFlabarin (Tb927.11.2410), a procyclic form (PCF) stage specific flagellar BAR domain protein. We named Tb927.11.2400 TbFlabarin like (TbFlabarinL) and demonstrate that it is a result of a gene duplication event, which occurred in African trypanosomes. TbFlabarinL is not essential for growth of the parasites under cell culture conditions and it is dispensable for developmental differentiation from BSF to the PCF in vitro. We generated a TbFlabarinL-specific antibody and showed that it localizes in the flagellum. The co-immunoprecipitation experiment together with a biochemical cell fractionation indicated a dual association of TbFlabarinL with the flagellar membrane and the components of the paraflagellar rod.},
  subject      = {Trypanosoma brucei},
  language  = {en}
}