Proteome Alterations
of Hippocampal Cells Caused by <i>Clostridium botulinum</i> C3 Exoenzyme
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Abstract
C3bot
from <i>Clostridium botulinum</i> is a bacterial
mono-ADP-ribosylating enzyme, which transfers an ADP-ribose moiety
onto the small GTPases Rho A/B/C. C3bot and the catalytic inactive
mutant (C3E174Q) cause axonal and dendritic growth as well as branching
in primary hippocampal neurons. In cultured murine hippocampal HT22
cells, protein abundances were analyzed in response to C3bot or C3E174Q
treatment using a shotgun proteomics approach. Proteome analyses were
performed at four time points over 6 days. More than 4000 protein
groups were identified at each time point and quantified in triplicate
analyses. On day one, 46 proteins showed an altered abundance, and
after 6 days, more than 700 proteins responded to C3bot with an up-
or down-regulation. In contrast, C3E174Q had no provable impact on
protein abundance. Protein quantification was verified for several
proteins by multiple reaction monitoring. Data analysis of altered
proteins revealed different cellular processes that were affected
by C3bot. They are particularly involved in mitochondrial and lysosomal
processes, adhesion, carbohydrate and glucose metabolism, signal transduction,
and nuclear proteins of translation and ribosome biogenesis. The results
of this study gain novel insights into the function of C3bot in hippocampal
cells