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- W2133905087 abstract "Human pathogen group A streptococcus (GAS) can take up heme from host heme-containing proteins as a source of iron. Little is known about the heme acquisition mechanism in GAS. We recently identified a streptococcal cell surface protein (designated Shp) and the lipoprotein component (designated HtsA) of an ATP-binding cassette (ABC) transporter made by GAS as heme-binding proteins. In an effort to delineate the molecular mechanism involved in heme acquisition by GAS, heme-free Shp (apo-Shp) and HtsA (apo-HtsA) were used to investigate heme transfer from heme-containing proteins (holo proteins) to the apo proteins. In addition, the interaction between holo-Shp and holo-HtsA was examined using native polyacrylamide gel electrophoresis. Heme was efficiently transferred from holo-Shp to apo-HtsA but not from holo-HtsA to apo-Shp. Apo-Shp acquired heme from human hemoglobin, and holo-Shp and holo-HtsA were able to form a complex, suggesting that Shp actively relays heme from hemoglobin to apo-HtsA. These findings demonstrate for the first time complex formation and directional heme transfer between a cell surface heme-binding protein and the lipoprotein of a heme-specific ABC transporter in gram-positive bacteria." @default.
- W2133905087 created "2016-06-24" @default.
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- W2133905087 date "2005-08-01" @default.
- W2133905087 modified "2023-10-17" @default.
- W2133905087 title "Heme Transfer from Streptococcal Cell Surface Protein Shp to HtsA of Transporter HtsABC" @default.
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- W2133905087 doi "https://doi.org/10.1128/iai.73.8.5086-5092.2005" @default.
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