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Infection and Immunity, February 2001, p. 1215-1220, Vol. 69, No. 2
Department of Microbiology and Immunology,
Emory University Health Sciences Center, Atlanta, Georgia 30322
Received 8 August 2000/Returned for modification 17 October
2000/Accepted 14 November 2000
The Mga protein in B514Sm, a Streptococcus pyogenes
strain isolated as a mouse pathogen, contains amino acid substitutions at conserved sites that render the protein defective. Replacement of
mga50 with the functional homolog mga4.1
restored full expression of Mga-regulated proteins. Restoration of Mga
function did not affect fibrinogen binding, nor did it affect virulence
in several mouse models of group A streptococcus infection.
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.2.1215-1220.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Restoration of Mga Function to a
Streptococcus pyogenes Strain (M Type 50) That Is Virulent
in Mice


and
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, 3001 Rollins Res. Center, Emory University Health Sciences Center, Atlanta GA 30322. Phone: (404) 727-0402. Fax:
(404) 727-8999. E-mail: scott{at}microbio.emory.edu.
Present address: Division of Infectious Diseases, Department of
Pediatrics, Children's Hospital and Regional Medical Center, Seattle,
WA 98105.
Present address: Department of Microbiology, University of Texas
Southwestern Medical Center, Dallas, TX 75390-9048.
§
Present address: Medical College of Georgia, School of Medicine,
Augusta, GA 30912.
Present address: Sackler Institute of Graduate Biomedical
Sciences, NYU School of Medicine, New York, NY 10016.
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