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J Biol Chem, Vol. 273, Issue 23, 14503-14515, June 5, 1998
From the Laboratory of Bacterial Pathogenesis and Immunology, The
Rockefeller University, New York, New York 10021
The plasmin(ogen) binding property of group A
streptococci is incriminated in tissue invasion processes. We have
characterized a novel 45-kDa protein displaying strong plasmin(ogen)
binding activity from the streptococcal surface. Based on its
biochemical properties, we confirmed the identity of this protein as
-Enolase, a Novel Strong Plasmin(ogen) Binding Protein on the
Surface of Pathogenic Streptococci
-enolase, a key glycolytic enzyme. Dose-dependent
-enolase activity, immune electron microscopy of whole streptococci
using specific antibodies, and the opsonic nature of polyclonal and
monoclonal antibodies concluded the presence of this protein on the
streptococcal surface. We, henceforth, termed the 45-kDa protein, SEN
(streptococcal surface enolase). SEN is found
ubiquitously on the surface of most streptococcal groups and serotypes
and showed significantly greater plasmin(ogen) binding affinity
compared with previously reported streptococcal plasminogen binding
proteins. Both the C-terminal lysine residue of SEN and a region
N-terminal to it play a critical role in plasminogen binding. Results
from competitive plasminogen binding inhibition assays and
cross-linking studies with intact streptococci indicate that SEN
contributes significantly to the overall streptococcal ability to bind
plasmin(ogen). Our findings, showing both the protected protease
activity of SEN-bound plasmin and SEN-specific immune responses,
provide evidence for an important role of SEN in the disease process
and post-streptococcal autoimmune diseases.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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B. Modun and P. Williams The Staphylococcal Transferrin-Binding Protein Is a Cell Wall Glyceraldehyde-3-Phosphate Dehydrogenase Infect. Immun., March 1, 1999; 67(3): 1086 - 1092. [Abstract] [Full Text] [PDF]
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W. W. Navarre and O. Schneewind Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope Microbiol. Mol. Biol. Rev., March 1, 1999; 63(1): 174 - 229. [Abstract] [Full Text] [PDF]
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