Isolation of a hemin and hemoglobin binding outer membrane protein of Vibrio vulnificus biotype 2 (serogroup E).
The eel pathogen Vibrio vulnificus biotype 2 (serogroup E) is able to use hemin (Hm) or hemoglobin (Hb) as the sole iron source for growth in vitro and in vivo. The mechanism of heme-iron acquisition in this bacterium requires a direct interaction through binding sites on the bacterial surface (constitutive outer membrane proteins). Using affinity chromatography techniques, a unique protein of around 36.5 kDa was isolated from cell envelopes of E86 strain regardless of the affinity ligand used, hemoglobin or hemin. This protein was purified from both iron-enriched and iron-restricted grown cells. These results support the hypothesis that in this pathogen Hm- and Hb-iron acquisition is mediated by a common protein receptor which recognizes the heme prosthetic group of Hb.
Fouz
B
B
Departamento de Microbiología y Parasitología, Facultad de Ciencias, Universidad de Santiago de Compostela. Lugo, Spain.
Mazoy
R
R
Vázquez
F
F
Lemos
M L
ML
Amaro
C
C
D001425:Bacterial Outer Membrane Proteins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D015153:Blotting, Western; D002853:Chromatography, Liquid; D006427:Hemin / Q000378:metabolism* / Q000494:pharmacology; D006454:Hemoglobins / Q000378:metabolism* / Q000494:pharmacology; D007501:Iron / Q000378:metabolism; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000819:agonists / Q000032:analysis / Q000302:isolation & purification; D012685:Sepharose; D014733:Vibrio / Q000737:chemistry* / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D006454:Hemoglobins; D011956:Receptors, Cell Surface; C028027:heme receptor; D006427:Hemin; D012685:Sepharose; D007501:Iron