ArticleProceedings of the National Academy of Sciences of the United States of America1994
Arrest of Listeria movement in host cells by a bacterial ActA analogue: implications for actin-based motility.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- Listeria monocytogenes hijacks CD147 to ensure proper membrane protrusion formation and efficient bacterial dissemination.Cellular and molecular life sciences : CMLS · 2019Article
- Miniature protein ligands for EVH1 domains: interplay between affinity, specificity, and cell motility.Biochemistry · 2007Article
- Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.The EMBO journal · 2007Article
- A plant-specific protein essential for blue-light-induced chloroplast movements.Plant physiology · 2005Article
- A role for VASP in RhoA-Diaphanous signalling to actin dynamics and SRF activity.The EMBO journal · 2003Article
- The cell biology of Listeria monocytogenes infection: the intersection of bacterial pathogenesis and cell-mediated immunity.The Journal of cell biology · 2002Review
- Actin-based motility of intracellular microbial pathogens.Microbiology and molecular biology reviews : MMBR · 2001Review
- Vaccinia locomotion in host cells: evidence for the universal involvement of actin-based motility sequences ABM-1 and ABM-2.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Gelsolin, a protein that caps the barbed ends and severs actin filaments, enhances the actin-based motility of Listeria monocytogenes in host cells.Infection and immunity · 1998Article
- Listeria and Shigella actin-based motility in host cells.Transactions of the American Clinical and Climatological Association · 1998Review
- Vinculin proteolysis unmasks an ActA homolog for actin-based Shigella motility.The Journal of cell biology · 1997Article
- A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family.The EMBO journal · 1997Article
- Cell motility driven by actin polymerization.Biophysical journal · 1996Article
- The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin.The Journal of cell biology · 1996Article
- The ActA polypeptides of Listeria ivanovii and Listeria monocytogenes harbor related binding sites for host microfilament proteins.Infection and immunity · 1996Article
- Recognition of two classes of oligoproline sequences in profilin-mediated acceleration of actin-based Shigella motility.The Journal of cell biology · 1996Article
- Detection and characterization by differential PCR of host eukaryotic cell genes differentially transcribed following uptake of intracellular bacteria.Infection and immunity · 1996Article
- Actin-based movement of Listeria monocytogenes: actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface.The Journal of cell biology · 1995Article
- Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function.The EMBO journal · 1995Article
- A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells.The EMBO journal · 1995Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Upon entering the host cell's cytoplasm, the pathogen Listeria monocytogenes can subvert the normal contractile system of the host cell; subsequent assembly of polar actin-filament structures is likely to provide the force for rapid intracellular bacterial movement and its cell-to-cell spread. We have now investigated the functional consequences of microinjecting Listeria-infected PtK2 cells with a synthetic peptide, CFEFPPPPTDE. This peptide represents one of four related oligoproline stretches in ActA, a bacterial surface protein necessary for Listeria-induced actin assembly. Over an estimated intracellular concentration range of 80 nM to 0.8 microM, this analogue rapidly blocks the formation of the actin-filament tails and arrests intracellular bacterial motility. Over the same time scale and concentration range, introduction of the ActA analogue also causes host cell membrane retraction. Bodipyphallacidin staining reveals that microinjection of the ActA analogue results in massive retraction of the actin cytoskeleton. Microinjection of 1-20 microM poly(L-proline) (intracellular concentration) fails to block Listeria intracellular movement or polar actin-filament assembly. As observed with ActA, however, poly(L-proline) does cause membrane retraction. Our findings demonstrate the efficacy of low molecular weight peptides in efforts to distinguish mechanistic features in Listeria motility and PtK2 host cell membrane reorganization. These observations also suggest that a cytoskeletal component sensitive to specific oligoproline peptides may participate in protein-protein interactions essential for both of these actin-associated processes.
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