Crosslinking of actin filaments and inhibition of actomyosin subfragment-1 ATPase activity by streptococcal M6 protein |
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| Authors: | J M Chalovich V A Fischetti |
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| Affiliation: | 1. Department of Biochemistry, East Carolina University School of Medicine, Greenville, North Carolina 27834, U.S.A.;2. Laboratory of Bacteriology and Immunology, The Rockefeller University, New York, New York 10021 U.S.A.;1. Program in Cell Biology, Peter Gilgan Centre for Research and Learning, Hospital for Sick Children, 686 Bay Street, 19-9800, Toronto, ON M5G 0A4, Canada;2. Keenan Research Centre of the Li Ka Shing Knowledge Institute, St. Michael’s Hospital, 290 Victoria Street, Toronto, ON M5C 1N8, Canada;1. Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60607, USA;2. Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, Chicago, IL 60607, USA;3. Center for Biomolecular Sciences, University of Illinois at Chicago, Chicago, IL 60607, USA;1. Department of Clinical Microbiology, Rigshospitalet, Copenhagen, Denmark;2. Costerton Biofilm Center, Institute of Immunology and Microbiology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark;3. Department of Infectious Diseases, Rigshospitalet, Copenhagen, Denmark;1. Program in Cell Biology, Hospital for Sick Children, 686 Bay Street, Toronto, Ontario M5G 0A4, Canada;2. Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada;3. Keenan Research Centre of the Li Ka Shing Knowledge Institute, St. Michael’s Hospital, 290 Victoria Street, Toronto, Ontario M5C 1N8, Canada;1. Faculty of Biological Sciences, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK;2. Fraunhofer Institute for Toxicology and Experimental Medicine, Nikolai-Fuchs-Straße 1, 30625 Hannover, Germany;3. Member of the German Center for Lung Research (DZL), Biomedical Research in Endstage and Obstructive Lung Disease Hannover (BREATH) Research Network, Hannover, Germany;4. Department of Dermatology and Allergy, University of Bonn, Bonn 53012, Germany;5. Division of Infection, Immunity & Respiratory Medicine, University of Manchester, Manchester M13 9PL, UK;6. Division of Microbiology and Infectious Diseases, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan;7. Faculty of Biology Medicine and Health, School of Biological Sciences, University of Manchester and Manchester Academic Health Science Centre, Manchester M13 9PL, UK;8. Faculty of Medicine and Health, Leeds Institute of Rheumatic and Musculoskeletal Medicine, University of Leeds, Leeds LS2 9JT, UK;9. Leeds Biomedical Research Centre, National Institute for Health Research, Leeds Teaching Hospitals, Leeds, UK |
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| Abstract: | M proteins are antiphagocytic molecules on the surface of group A streptococci having physical characteristics similar to those of mammalian tropomyosin. Both are alpha-helical coiled-coil fibrous structures with a similar seven-residue periodicity of nonpolar and charged amino acids. To determine if M protein is functionally similar to tropomyosin we studied the interaction of M protein with F-actin. At low ionic strength, M protein binds to actin weakly with a stoichiometry different from that of tropomyosin. M protein does not compete with tropomyosin for the binding to actin, indicating that it is functionally different from tropomyosin. M protein does compete with myosin subfragment-1 for binding to actin and induces the formation of bundles of actin filaments. The formation of actin aggregates is associated with a sharp reduction in the rate of ATP hydrolysis by subfragment-1. Intact streptococci having M protein on their surface are shown to bind to actin. |
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