Disease relevance of Rhizoferrin

• The deduced protein encoded by pvuA displayed the highest similarity (31% identity; 48% similarity) to RumA, a ferric rhizoferrin receptor of Morganella morganii [1].
• Transport and utilization of rhizoferrin bound iron in Mycobacterium smegmatis [2].

High impact information on Rhizoferrin

• Analysis of a 10-kb sequence flanking rumA and rumB on both sides revealed seven additional open reading frames for which no role in ferric rhizoferrin uptake could be discerned [3].
• Additional genes required for ferric rhizoferrin translocation across the cytoplasmic membrane must map at sites distinct from rumA and rumB [3].
• Transport and metabolization of iron bound to the fungal siderophore rhizoferrin was analyzed by transport kinetics, Mössbauer and EPR spectroscopy [2].
• Quantification of siderophores using standard compounds deferrioxamine mesylate and rhizoferrin revealed that Phanerochaete chrysosporium produced maximum among the hydroxamate producing fungi and Mycotypha africana resulted maximum among the carboxylate producing fungi [4].

Analytical, diagnostic and therapeutic context of Rhizoferrin

• We purified this siderophore by conventional column chromatography and high-pressure liquid chromatography and used mass spectrometric analysis to demonstrate that it is structurally similar to the polycarboxylate siderophore rhizoferrin [5].

References