Restoration of Mga function to a Streptococcus pyogenes strain (M type 50) that is virulent in mice

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...

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Published inInfection and immunity Vol. 69; no. 2; pp. 1215 - 1220
Main Authors LIMBAGO, Brandi, MCIVER, Kevin S, PENUMALLI, Vikram, WEINRICK, Brian, SCOTT, June R
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.02.2001
SeriesNote
Subjects
Animals
Antigens, Bacterial
Bacterial diseases
Bacterial Outer Membrane Proteins
Bacterial Proteins - metabolism
Bacterial Proteins - physiology
Bacteriology
Biological and medical sciences
Carrier Proteins - metabolism
Experimental bacterial diseases and models
Fibrinogen - metabolism
Fundamental and applied biological sciences. Psychology
Infectious diseases
Medical sciences
mga gene
Mga protein
Mice
Mice, Inbred C57BL
Microbiology
Molecular Pathogenesis
Molecular Weight
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Streptococcal Infections - etiology
Streptococcus pyogenes
Streptococcus pyogenes - pathogenicity
Virulence
Rodentia
Replacement
Protein A
Infection
Streptococcaceae
Vertebrata
Type
Mammalia
Restoration
Mouse
Substitution
Aminoacid
Pathogenic
Streptococcal infection
Pathogen strain
Streptococcus A
Bacteriosis
Bacteria
Micrococcales
Isolate
Isolation
Streptococcus pyogenes
Regulation
Defectivity
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Summary: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.
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Present address: Division of Infectious Diseases, Department of Pediatrics, Children's Hospital and Regional Medical Center, Seattle, WA 98105.
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.
Present address: Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9048.
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@microbio.emory.edu.
ISSN:0019-9567
1098-5522
DOI:10.1128/IAI.69.2.1215-1220.2001