Detection of heme-binding proteins in epidemic strains of Burkholderia cepacia

A panel of 30 previously characterized strains representing five genomovars from the Burkholderia cepacia complex (E, Mahenthiralingam, T, Coenye, J. W. Chung, D, P, Speert, J. R, W, Govan, P, Taylor, and P, Vandamme, J, Clin , Microbiol. 38:910-913, 2000) were examined for their iron protoporphyrin IX-binding ability. These included B. cepacia genomovars I and III and B, s tabilis (formerly B. cepacia genomovar IV), B, multivorans (formerly B, cep acia genomovar II), and B, vietnamiensis (formerly B, cepacia genomovar V), Cells were exposed to mu -ore bisheme of iron protoporphyrin IX (mu -oxo d imers) and examined by sodium dodecyl sulfate-polyacrylamide gel electropho resis under nonreducing, nondenaturing conditions for the presence of heme- binding proteins using tetramethylbenzidine-H2O2 staining. Seven of the 30 strains, each belonging to B. cepacia genomovar III and designated epidemic (in possessing the B, cepacia epidemic strain marker), expressed a 96- to 100-kDa heme-binding protein which was located in the outer membrane. The h eme-binding protein of B, cepacia genomovar III epidemic strain C5424 bound iron(III) protoporphyrin IX in both the monomeric and mu -oxo bisheme form s. Cells of all strains grown on Columbia agar bound iron protoporphyrin IX in the Ir-oxo bisheme (dimeric) form. There were no statistical difference s between the five genomovars, or those possessing the heme-binding protein , in their Cr-oxo bisheme-binding ability. Possession of the outer membrane heme-binding protein may be a pathogenicity trait in enabling the bacteriu m to withstand oxidative stresses in inflammatory exudates in the lung and may aid identification of invasive epidemic strains of B, cepacia.