Molecular characterization of iron binding proteins, transferrin and ferritin heavy chain subunit, from the bumblebee Bombus ignitus

Author(s):  
Dong Wang ◽  
Bo Yeon Kim ◽  
Kwang Sik Lee ◽  
Hyung Joo Yoon ◽  
Zheng Cui ◽  
...  
1999 ◽  
Vol 67 (4) ◽  
pp. 2035-2039 ◽  
Author(s):  
Jovana Gobin ◽  
Diane K. Wong ◽  
Bradford W. Gibson ◽  
Marcus A. Horwitz

ABSTRACT Pathogenic mycobacteria must acquire iron in the host in order to multiply and cause disease. To do so, they release abundant quantities of siderophores called exochelins, which have the capacity to scavenge iron from host iron-binding proteins and deliver it to the mycobacteria. In this study, we have characterized the exochelins of Mycobacterium bovis, the causative agent of bovine and occasionally of human tuberculosis, and the highly attenuated descendant of M. bovis, bacillus Calmette-Guérin (BCG), widely used as a vaccine against human tuberculosis. The M. bovis type strain, five substrains ofM. bovis BCG (Copenhagen, Glaxo, Japanese, Pasteur, and Tice), and two strains of virulent Mycobacterium tuberculosis all produce the same set of exochelins, although the relative amounts of individual exochelins may differ. Among these mycobacteria, the total amount of exochelins produced is greatest in M. tuberculosis, intermediate in M. bovis, and smallest in M. bovis BCG.


1976 ◽  
Vol 66 (3) ◽  
pp. 447-455 ◽  
Author(s):  
Helmut HUEBERS ◽  
Eiko HUEBERS ◽  
Walter RUMMEL ◽  
Robert R. CRICHTON

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