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Infection and Immunity, July 2007, p. 3581-3593, Vol. 75, No. 7
0019-9567/07/$08.00+0     doi:10.1128/IAI.00214-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Adapter Protein SH2-Bß Stimulates Actin-Based Motility of Listeria monocytogenes in a Vasodilator-Stimulated Phosphoprotein (VASP)-Dependent Fashion{triangledown}

Maria Diakonova,1,{dagger}* Emmanuele Helfer,3,{dagger} Stephanie Seveau,2,{ddagger} Joel A. Swanson,2 Christine Kocks,4 Liangyou Rui,1 Marie-France Carlier,3 and Christin Carter-Su1

Departments of Molecular and Integrative Physiology,1 Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan,2 Dynamique du Cytosquelette Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Gif-sur-Yvette, France,3 Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts4

Received 8 February 2007/ Returned for modification 20 March 2007/ Accepted 10 April 2007

SH2-Bß (Src homology 2 Bß) is an adapter protein that is required for maximal growth hormone-dependent actin reorganization in membrane ruffling and cell motility. Here we show that SH2-Bß is also required for maximal actin-based motility of Listeria monocytogenes. SH2-Bß localizes to Listeria-induced actin tails and increases the rate of bacterial propulsion in infected cells and in cell extracts. Furthermore, Listeria motility is decreased in mouse embryo fibroblasts from SH2-B–/– mice. Both recruitment of SH2-Bß to Listeria and SH2-Bß stimulation of actin-based propulsion require the vasodilator-stimulated phosphoprotein (VASP), which binds ActA at the surfaces of Listeria cells and enhances bacterial actin-based motility. SH2-Bß enhances actin-based movement of ActA-coated beads in a biomimetic actin-based motility assay, provided that VASP is present. In vitro binding assays show that SH2-Bß binds ActA but not VASP; however, binding to ActA is greater in the presence of VASP. Because VASP also plays an essential regulatory role in actin-based processes in eukaryotic cells, the present results provide mechanistic insight into the functions of both SH2-Bß and VASP in motility and also increase our understanding of the fundamental mechanism by which Listeria spreads.

* Corresponding author. Present address: Department of Biological Sciences, University of Toledo, 2801 W. Bancroft Street, Toledo, OH 43606-3390. Phone: (419) 530-7876. Fax: (419) 530-7737. E-mail: mdiakon{at}utnet.utoledo.edu

{triangledown} Published ahead of print on 23 April 2007.

Editor: J. B. Bliska

{dagger} M.D. and E.H. contributed equally to this work.

{ddagger} Present address: Departments of Microbiology & Internal Medicine, Ohio State University, Columbus, OH.

Infection and Immunity, July 2007, p. 3581-3593, Vol. 75, No. 7
0019-9567/07/$08.00+0     doi:10.1128/IAI.00214-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rider, L., Tao, J., Snyder, S., Brinley, B., Lu, J., Diakonova, M. (2009). Adapter Protein SH2B1{beta} Cross-Links Actin Filaments and Regulates Actin Cytoskeleton. Mol. Endocrinol. 23: 1065-1076 [Abstract] [Full Text]  


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