Site-specific rate constants for iron acquisition from transferrin by the Aspergillus fumigatus siderophores N′,N′′,N′′′-triacetylfusarinine C and ferricrocin

2005 ◽  
Vol 10 (3) ◽  
pp. 211-220 ◽  
Author(s):  
A. H. T. Hissen ◽  
M. M. Moore
2014 ◽  
Vol 16 (24) ◽  
pp. 12183-12193 ◽  
Author(s):  
Jihad Badra ◽  
Ahmed E. Elwardany ◽  
Aamir Farooq

Reaction rate constants of the reaction of four large ketones with hydroxyl (OH) are investigated behind reflected shock waves using OH laser absorption.


2004 ◽  
Vol 72 (3) ◽  
pp. 1402-1408 ◽  
Author(s):  
A. H. T. Hissen ◽  
J. M. T. Chow ◽  
L. J. Pinto ◽  
M. M. Moore

ABSTRACT Aspergillus fumigatus is a filamentous fungus which can cause invasive disease in immunocompromised individuals. A. fumigatus can grow in medium containing up to 80% human serum, despite very low concentrations of free iron. The purpose of this study was to determine the mechanism by which A. fumigatus obtains iron from the serum iron-binding protein transferrin. In iron-depleted minimal essential medium (MEM), A. fumigatus growth was supported by the addition of holotransferrin (holoTf) or FeCl3 but not by the addition of apotransferrin (apoTf). Proteolytic degradation of transferrin by A. fumigatus occurred in MEM-serum; however, transferrin degradation did not occur until late logarithmic phase. Moreover, transferrin was not degraded by A. fumigatus incubated in MEM-holoTf. Urea polyacrylamide gel electrophoresis showed that in MEM-holoTf, holoTf was completely converted to apoTf by A. fumigatus. In human serum, all of the monoferric transferrin was converted to apoTf within 8 h. Siderophores were secreted by A. fumigatus after 8 h of growth in MEM-serum and 12 h in MEM-holoTf. The involvement of small molecules in iron acquisition was confirmed by the fact that transferrin was deferrated by A. fumigatus even when physically separated by a 12-kDa-cutoff membrane. Five siderophores were purified from A. fumigatus culture medium, and the two major siderophores were identified as triacetylfusarinine C and ferricrocin. Both triacetylfusarinine C and ferricrocin removed iron from holoTf with an affinity comparable to that of ferrichrome. These data indicate that A. fumigatus survival in human serum in vitro involves siderophore-mediated removal of iron from transferrin. Proteolytic degradation of transferrin may play a secondary role in iron acquisition.


2003 ◽  
Vol 380 (1-2) ◽  
pp. 88-94 ◽  
Author(s):  
Bryan G. Reuben ◽  
Ya’acov Ritov ◽  
Orit Geller ◽  
Melinda A. McFarland ◽  
Alan G. Marshall ◽  
...  

2010 ◽  
Vol 78 (4) ◽  
pp. 1038-1054 ◽  
Author(s):  
Hong Liu ◽  
Fabrice N. Gravelat ◽  
Lisa Y. Chiang ◽  
Dan Chen ◽  
Ghyslaine Vanier ◽  
...  

2014 ◽  
Vol 139 ◽  
pp. 30-37 ◽  
Author(s):  
Etelka Farkas ◽  
Orsolya Szabó ◽  
Péter L. Parajdi-Losonczi ◽  
György Balla ◽  
István Pócsi

2009 ◽  
Vol 75 (12) ◽  
pp. 4194-4196 ◽  
Author(s):  
Anja Wallner ◽  
Michael Blatzer ◽  
Markus Schrettl ◽  
Bettina Sarg ◽  
Herbert Lindner ◽  
...  

ABSTRACT Iron is an essential metal for virtually all organisms. Iron acquisition is well characterized for various organisms, whereas intracellular iron distribution is poorly understood. In contrast to bacteria, plants, and animals, most fungi lack ferritin-mediated iron storage but possess an intracellular siderophore shown to be involved in iron storage. Here we demonstrate that deficiency in the intracellular siderophore ferricrocin causes iron starvation in conidia of Aspergillus fumigatus, demonstrating that ferricrocin is also involved in intra- and transcellular iron distribution. Thus, ferricrocin represents the first intracellular iron transporter identified in any organism.


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