ArticleThe Journal of cell biology1996
Recognition of two classes of oligoproline sequences in profilin-mediated acceleration of actin-based Shigella motility.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 67 citations in OpenAlex.
- Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly.Nature communications · 2017Article
- Myosin-X facilitates Shigella-induced membrane protrusions and cell-to-cell spread.Cellular microbiology · 2013Article
- Bacillus anthracis edema toxin impairs neutrophil actin-based motility.Infection and immunity · 2009Article
- Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.The EMBO journal · 2007Article
- Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- CapG(-/-) mice have specific host defense defects that render them more susceptible than CapG(+/+) mice to Listeria monocytogenes infection but not to Salmonella enterica serovar Typhimurium infection.Infection and immunity · 2003Article
- Effects of ectopically expressed neuronal Wiskott-Aldrich syndrome protein domains on Rickettsia rickettsii actin-based motility.Infection and immunity · 2003Article
- Contribution of Ena/VASP proteins to intracellular motility of listeria requires phosphorylation and proline-rich core but not F-actin binding or multimerization.Molecular biology of the cell · 2002Article
- Clamped-filament elongation model for actin-based motors.Biophysical journal · 2002Article
- Actin-based motility of intracellular microbial pathogens.Microbiology and molecular biology reviews : MMBR · 2001Review
- Burkholderia pseudomallei induces cell fusion and actin-associated membrane protrusion: a possible mechanism for cell-to-cell spreading.Infection and immunity · 2000Article
- Rho family GTPase Cdc42 is essential for the actin-based motility of Shigella in mammalian cells.The Journal of experimental medicine · 2000Article
- Profilin is required for optimal actin-dependent transcription of respiratory syncytial virus genome RNA.Journal of virology · 2000Article
- 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
- Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri.The EMBO journal · 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
- The isolated comet tail pseudopodium of Listeria monocytogenes: a tail of two actin filament populations, long and axial and short and random.The Journal of cell biology · 1997Article
- The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences.The EMBO journal · 1997Article
- Enteropathogenic E. coli, Salmonella, and Shigella: masters of host cell cytoskeletal exploitation.Emerging infectious diseasesReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The gram negative rod Shigella flexneri uses it surface protein IcsA to induce host cell actin assembly and to achieve intracellular motility. Yet, the IcsA protein lacks the oligoproline sequences found in ActA, the surface protein required for locomotion of the gram positive rod Listeria monocytogenes. Microinjection of a peptide matching the second ActA oligoproline repeat (FEFPPPPTDE) stops Listeria locomotion (Southwick, F.S., and D.L. Purich. 1994a. Proc. Natl. Acad. Sci. USA. 91:5168-5172), and submicromolar concentrations (intracellular concentration 80-800 nM) similarly arrest Shigella rocket-tail assembly and intracellular motility. Coinjection of a binary solution containing profilin and the ActA analogue increased the observed rates of intracellular motility by a factor of three (mean velocity 0.90 +/- 0.07 mu m/s, SD n=16 before injection vs 0.3 +/- 0.1 mu m/s, n=33 postinjection, intracellular concentration = 80 nM profilin plus 80 nM ActA analogue). Recent evidence suggests the ActA analogue may act by displacing the profilin-binding protein VASP (Pistor, S.C., T. Chakaborty, V. Walter, and J. Wehland. 1995. Curr. Biol. 5:517-525). At considerably higher intracellular concentrations (10 muM), the VASP oligoproline sequence (GPPPPP)3 thought to represent the profilin-binding site (Reinhard, M., K. Giehl, K. Abel, C. Haffner, T. Jarchau, V. Hoppe, B.M. Jockusch, and U. Walter. 1995. EMBO (Eur. Mol. Biol. Organ.) J. 14:1583-1589) also inhibited Shigella movement. A binary mixture of the VASP analogue and profilin (each 10 muM intracellular concentration) led to a doubling of Shigella intracellular migration velocity (0.09 +/- 0.06 mu m/s, n = 25 preinjection vs 0.18 +/- 0.10 mu m/s, n = 61 postinjection). Thus, the two structurally divergent bacteria, Listeria and Shigella, have adopted convergent mechanisms involving profilin recognition of VASP oligoproline sequences and VASP recognition of oligoproline sequences in ActA or an ActA-like host protein to induce host cell actin assembly and to provide the force for intracellular locomotion and cell-cell spread.
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