Identification of heme-binding proteins in the cell membranes of Vibrio anguillarum.
Two strains of Vibrio anguillarum belonging to O1 and O2 serotypes were examined for their ability to bind hemin and hemoglobin. Whole cells as well as membrane extracts from both strains could clearly bind hemin and hemoglobin constitutively. Hemoglobin binding was completely inhibited by a 100-fold excess of unlabelled hemoglobin and also by hemin, suggesting the existence of specific receptors for heme groups in the cell membranes. Several hemin-binding and hemoglobin-binding bands with similar molecular sizes were detected in polyacrylamide gels as well as in Western blots. Only two of these protein bands in both strains were iron-regulated while the others were independent of the cell iron status. We conclude that both serotypes of V. anguillarum possess heme-binding abilities by means of membrane proteins.
Mazoy
R
R
Departamento de Microbiología y Parasitología, Facultad de Ciencias, Universidad de Santiago de Compostela, Lugo, Spain.
Lemos
M L
ML
D001425:Bacterial Outer Membrane Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D002352:Carrier Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D006418:Heme / Q000378:metabolism; D000081062:Heme-Binding Proteins; D006420:Hemeproteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism; D008970:Molecular Weight; D014733:Vibrio / Q000737:chemistry* / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D000081062:Heme-Binding Proteins; D006420:Hemeproteins; D006454:Hemoglobins; D006418:Heme