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A crucial role for profilin–actin in the intracellular motility of Listeria monocytogenes
Author(s) -
Grenklo Staffan,
Geese Marcus,
Lindberg Uno,
Wehland Jürgen,
Karlsson Roger,
Sechi Antonio S
Publication year - 2003
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.embor823
Subject(s) - profilin , listeria monocytogenes , motility , actin , microbiology and biotechnology , biology , actin remodeling , listeria , mdia1 , actin binding protein , actin cytoskeleton , biochemistry , cytoskeleton , bacteria , genetics , cell
We have examined the effect of covalently crosslinked profilin–actin (PxA), which closely matches the biochemical properties of ordinary profilin–actin and interferes with actin polymerization in vitro and in vivo , on Listeria monocytogenes motility. PxA caused a marked reduction in bacterial motility, which was accompanied by the detachment of bacterial tails. The effect of PxA was dependent on its binding to proline‐rich sequences, as shown by the inability of P H133S xA, which cannot interact with such sequences, to impair Listeria motility. PxA did not alter the motility of a Listeria mutant that is unable to recruit Ena (Enabled)/VASP (vasodilator‐stimulated phosphoprotein) proteins and profilin to its surface. Finally, PxA did not block the initiation of actin‐tail formation, indicating that profilin–actin is only required for the elongation of actin filaments at the bacterial surface. Our findings provide further evidence that profilin–actin is important for actin‐based processes, and show that it has a key function in Listeria motility.