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A crucial role for profilin-actin in the intracellular motility of Listeria monocytogenes
Stockholm University, Faculty of Science, The Wenner-Gren Institute .
Department of Cell Biology, Gesellschaft für Biotechnologische Forschung (GBF).
Stockholm University, Faculty of Science, The Wenner-Gren Institute , Department of Cell Biology.
Department of Cell Biology, Gesellschaft für Biotechnologische Forschung (GBF).
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2003 (English)In: EMBO reports, ISSN 1469-221, Vol. 4, no 5, 523-529 p.Article in journal (Refereed) Published
Abstract [en]

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 PH133SxA, 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.

Place, publisher, year, edition, pages
London: Nature Publishing Group , 2003. Vol. 4, no 5, 523-529 p.
National Category
Cell Biology
Research subject
Cellbiology
Identifiers
URN: urn:nbn:se:su:diva-23150DOI: 10.1038/sj.embor.embor823OAI: oai:DiVA.org:su-23150DiVA: diva2:190412
Note
Part of urn:nbn:se:su:diva-168Available from: 2004-05-13 Created: 2004-05-13 Last updated: 2009-12-22Bibliographically approved
In thesis
1. Cross-linked Profilin:actin - A tool to study actin dynamics in non-muscle cells
Open this publication in new window or tab >>Cross-linked Profilin:actin - A tool to study actin dynamics in non-muscle cells
2004 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The microfilament system, consisting of actin and a number of auxiliary proteins, is fundamental for cell motility. Its dynamic organization depends on receptor-mediated signals, leading to rapid polymerizations and depolymerizations of actin. Profilin binds to non-filamentous actin, inhibits spontaneous filament formation, and functions as a regulator of actin polymerization. The profilin:actin complex, is thought to be the principal source of actin for filament formation although the role of profilin is not fully elucidated.

In this thesis, a cross-linked profilin:actin complex (PxA), that retains the properties of ordinary profilin:actin, except for being non-dissociable, has been used to characterize the role of profilin and profilin:actin in non-muscle cells. A rapid screening method, employing PxA and based on the far western technique and mass-spectrometry, was designed to identify cellular components that specifically bind profilin:actin. Microinjection of PxA into cells infected with the bacteria Listeria monocytogenes impaired bacterial motility but a mutant PxA, unable to bind proline-rich sequences had no effect, demonstrating that profilin:actin is vital for the activity of the actin polymer-forming complex that the pathogen recruits to its surface upon infection.

Fluorescence microscopy using two distinct sets of affinity-purified actin and profilin antibodies generated against PxA enabled localization of monomeric actin in cells. One of the actin and both profilin antibodies resulted in a dotted pattern of fluorescence partially aligning with microtubules whereas the other actin antibody detected filamentous actin. The result demonstrates extensive variability in epitope recognition, and indicates that unpolymerized actin, i.e. profilin:actin and maybe other complex-bound forms of actin, distributes in small packages that might be transported along microtubules. Microinjection of PxA into lamprey axons demonstrated the involvement of actin polymerization during synaptic signaling.

Place, publisher, year, edition, pages
Stockholm: Wenner-Grens institut för experimentell biologi, 2004. 64 p.
Keyword
actin dynamics, profilin, actin, Profilin-actin complex, Cell motility, synaptic vesicle trafficing, Far western, fluorescence microscopy
National Category
Cell Biology
Identifiers
urn:nbn:se:su:diva-168 (URN)91-7265-854-1 (ISBN)
Public defence
2004-06-04, De Geersalen, Geovetenskapens hus, Svante Arrhenius väg 8 A, Stockholm, 10:00
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Available from: 2004-05-13 Created: 2004-05-13 Last updated: 2012-01-12Bibliographically approved

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