Acquisition of iron from host proteins by the group A streptococcus.
To identify mammalian iron-binding proteins that can serve as iron sources for Streptococcus pyogenes, the group A streptococcus (GAS), we used a plate assay. Ferritin, hemin, hemoglobin, myoglobin, and catalase can support growth of GAS on iron-depleted medium. However, growth was not detected when iron was provided as iron-saturated transferrin or lactoferrin or bound to cytochrome c. Therefore, it appears that GAS can use the intracellular iron sources available in the human body, which is consistent with its ability to cause tissue destruction during infection.
Eichenbaum
Z
Z
Department of Microbiology and Immunology, Emory University, Atlanta, Georgia 30322, USA.
Muller
E
E
Morse
S A
SA
Scott
J R
JR
D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D006801:Humans; D007501:Iron / Q000378:metabolism*; D033862:Iron-Binding Proteins; D008322:Mammals; D013290:Streptococcal Infections / Q000378:metabolism*; D013297:Streptococcus pyogenes / Q000378:metabolism*; D033863:Transferrin-Binding Proteins
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D033862:Iron-Binding Proteins; D033863:Transferrin-Binding Proteins; D007501:Iron