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 Mga function did not affect fibrinogen binding, nor did it affect virulence in several mouse models of group A streptococcus infection.
Limbago
B
B
Department of Microbiology and Immunology, Emory University Health Sciences Center, Atlanta, Georgia 30322, USA.
McIver
K S
KS
Penumalli
V
V
Weinrick
B
B
Scott
J R
JR
D000818:Animals; D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000378:metabolism / Q000502:physiology*; D002352:Carrier Proteins / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D008970:Molecular Weight; D013290:Streptococcal Infections / Q000209:etiology; D013297:Streptococcus pyogenes / Q000472:pathogenicity*; D014774:Virulence
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; C014689:streptococcal M protein; C068267:mry protein, Streptococcus pyogenes; D005340:Fibrinogen