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Infection and Immunity, January 2004, p. 94-105, Vol. 72, No. 1
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.1.94-105.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Role of the C-Terminal Lysine Residues of Streptococcal Surface Enolase in Glu- and Lys-Plasminogen-Binding Activities of Group A Streptococci

Anne Derbise ,1,{dagger},{ddagger} Youngmia P. Song,2,{ddagger} Sonia Parikh,2 Vincent A. Fischetti,1 and Vijay Pancholi1,2*

Laboratory of Bacterial Pathogenesis, Public Health Research Institute, International Center for Public Health, Newark, New Jersey,2 Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York1

Received 18 July 2003/ Accepted 22 September 2003

Streptococcal surface enolase (SEN) is a major plasminogen-binding protein of group A streptococci. Our earlier biochemical studies have suggested that the region responsible for this property is likely located at the C-terminal end of the SEN molecule. In the present study, the gene encoding SEN was cloned from group A streptococci M6 isolate D471. A series of mutations in the sen gene corresponding to the C-terminal region (428KSFYNLKK435) of the SEN molecule were created by either deleting one or more terminal lysine residues or replacing them with leucine. All purified recombinant SEN proteins with altered C-terminal ends were found to be enzymatically active and were analyzed for their Glu- and Lys-plasminogen-binding activities. Wild-type SEN bound to Lys-plasminogen with almost three times more affinity than to Glu-plasminogen. However, the recombinant mutant SEN proteins with a deletion of Lys434-435 or with K435L and K434-435L replacements showed a significant decrease in Glu- and Lys-plasminogen-binding activities. Accordingly, a streptococcal mutant expressing SEN-K434-435L showed a significant decrease in Glu- and Lys-plasminogen-binding activities. Biochemical and functional analyses of the isogenic mutant strain revealed a significant decrease in its abilities to cleave a chromogenic tripeptide substrate, acquire plasminogen from human plasma, and penetrate the extracellular matrix. Together, these data indicate that the last two C-terminal lysine residues of surface-exposed SEN contribute significantly to the plasminogen-binding activity of intact group A streptococci and hence to their ability to exploit host properties to their own advantage in tissue invasion.

* Corresponding author. Mailing address: Laboratory of Bacterial Pathogenesis, Public Health Research Institute, International Center for Public Health, Room W450T, 225 Warren St., Newark, NJ 07103-3535. Phone: (973) 854-3430. Fax: (973) 854-3431. E-mail: pancholi{at}phri.org.

Editor: B. B. Finlay

{dagger} Present address: Unité de Bactériologie Moléculaire et Médicale, Laboratoire des Yersinia, Institut Pasteur, 75724 Paris Cedex 15, France.

{ddagger} A.D. and Y.P.S. contributed equally to this work.

Infection and Immunity, January 2004, p. 94-105, Vol. 72, No. 1
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.1.94-105.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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