Microbial Envelope Proteins Related to Iron

Neilands, J. B.

doi:10.1146/annurev.mi.36.100182.001441

Cited by 573 publications

(412 citation statements)

References 1 publication

Supporting

Mentioning

402

Contrasting

Unclassified

Order By: Relevance

“…400-2,000 Da), produced in iron deficient conditions by microorganisms, which bind and facilitate the transport of external iron into the cells via a high affinity system [11]. According to Neilands [12], siderophores can serve as an attachment site not only for iron but also for a variety of noxious agents including antibiotics and other drugs, which also could be translocated into the cell. That is why we suggest that TB and MB as well as other drugs could attach to a siderophore, link to a protein, and translocate together through the membrane.…”

Section: Introductionmentioning

confidence: 99%

Interaction of the photobactericides methylene blue and toluidine blue with a fluorophore in Pseudomonas aeruginosa cells

Усачева¹,

Teichert²,

Usachev

et al. 2008

Lasers Surg Med

View full text Add to dashboard Cite

Background and Objectives: The difference in photobactericidal efficacy between methylene blue (MB) and toluidine blue (TB) may be explained by their involvement with proteins, lipopolysaccharides (LPS), and siderophores and siderophore-receptor protein complexes on the bacterial outer membrane. This study aims to determine if this is the case by using the fluorescence given off by a pseudomonal siderophore named pyoverdin. Study Design/Materials and Methods: Confocal laser scanning microscopy was used to observe the fluorescence of Pseudomonas aeruginosa cells excited at 488 nm in the presence of increasing dye concentrations. Results: Cellular fluorescence at 522 nm progressively decreased with increasing dye concentrations. The SternVolmer constants for cellular fluorescence quenching with the dyes were compared to the association constants for dyes complexed with LPS. The quenching of cellular fluorescence was associated with the formation of a ground-state complex between the dyes and pyoverdin-FpvA protein system. MB readily complexed with this system, whereas TB complexed more strongly with LPS. Conclusion: The different affinities of the dyes for both pyoverdin-protein and LPS will affect the contributions of the dyes' interactions with these biopolymers to the overall bacterial photodamage.

show abstract

Section: Introductionmentioning

confidence: 99%

Interaction of the photobactericides methylene blue and toluidine blue with a fluorophore in Pseudomonas aeruginosa cells

Усачева¹,

Teichert²,

Usachev

et al. 2008

Lasers Surg Med

View full text Add to dashboard Cite

show abstract

“…The ferrisiderophore complex is then usually translocated through the cell membranes by a highly specific active transport system involving several specialized proteins, the best characterized being the iron-regulated outer-membrane proteins (IROMPs) which act as ferrisiderophore receptors (Neilands, 1982). Iron-starved Escherichia coli cells synthesize several such IROMPs, each recognizing usually one (ferri)siderophore, including the endogenous siderophore produced by this bacterium, enterobactin, as well as the iron complexes of desferriferrichrome, desferriferrichrysin, coprogen or rhodotorulic acid, siderophores synthesized by other micro-organisms (Braun et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Exogenous siderophore-mediated iron uptake in Pseudomonas aeruginosa: possible involvement of porin OprF in iron translocation

Meyer¹

1992

Journal of General Microbiology

View full text Add to dashboard Cite

In addition to the two siderophores pyoverdine and pyochelin synthesized by Pseudomonas aeruginusu ATCC 15692 (strain PAOl), several siderophores produced by other bacteria or fungi, namely cepabactin, salicylic acid, desferriferrichrysin, desferriferricrocin, desferriferrioxamine B, desferriferrioxamine E and coprogen, were able to promote iron uptake with variable efficiencies into this bacterium. For most of these siderophores, these results were consistent with the growth stimulation produced by the same compounds in a plate bioassay. Desferriferriduome A, enterobactin and desferriferrirubin, however, did not promote iron uptake, although enterobactin and desferriferrirubin stimulated bacterial growth. These paradoxical data are discussed in view of siderophore-inducible iron uptake systems, as demonstrated recently for enterobactin. Among the strains tested, including the wild-type PAO1, the pyoverdine-less mutant PA06606 and the two porin-mutants P. ueruginusu H636 (oprl;: : a) and P. ueruginosu H673 (oprD: : Tn501), only for the porin-OprF mutant were fewer siderophores able to promote iron uptake compared to the other strains. Such results suggest that beside specific routes for iron uptake P. aerughsu is also able to take up siderophore-liganded iron through OprF.

show abstract

“…These proteins have association constants for ferric ion of more than 1022 and are normally only partly saturated (7). To scavenge this essential nutrient from such a hostile iron-restricted environment, many bacterial pathogens produce and secrete low-molecular-weight, Fe (III)-specific ligands, termed siderophores, and express cognate cell surface receptors which bind respective ferric siderophore complexes as the first step in the iron uptake pathway (3,13,25,26,32). Therefore, the ability to utilize the protein-bound iron in vivo has been frequently associated with bacterial pathogenesis (13,28).…”

mentioning

confidence: 99%

Siderophore‐Mediated Utilization of Iron Bound to Transferrin by Vibrio parahaemolyticus

Yamamoto

Okujo

Matsuura

et al. 1994

Microbiology and Immunology

View full text Add to dashboard Cite

Vibrio parahaemolyticus produces a structurally novel type of siderophore, termed vibrioferrin, in response to iron-limitation. This study was performed to examine whether vibrioferrin can assimilate iron from human iron-binding proteins for growth. Comparison of the growth rates between V. parahaemolyticus AQ 3354 and its spontaneously arising, vibrioferrindeficient mutant revealed that vibrioferrin was able to sequester iron from 30% iron-saturated human transferrin for growth, but not from human lactoferrin even if fully saturated with iron. In both strains, iron limitation induced two high-molecular-weight outer membrane proteins with apparent molecular masses of approximately 78 and 83 kDa. Since only the outer membrane fraction including these proteins showed a binding capacity to ferric vibrioferrin complex, either of them may function as its cell surface receptor. These results suggested that the organism might utilize such a source of host iron through the action of vibrioferrin during in vivo survival and proliferation, although its importance in pathogenesis is unknown.

show abstract

Microbial Envelope Proteins Related to Iron

Cited by 573 publications

References 1 publication

Interaction of the photobactericides methylene blue and toluidine blue with a fluorophore in Pseudomonas aeruginosa cells

Interaction of the photobactericides methylene blue and toluidine blue with a fluorophore in Pseudomonas aeruginosa cells

Exogenous siderophore-mediated iron uptake in Pseudomonas aeruginosa: possible involvement of porin OprF in iron translocation

Siderophore‐Mediated Utilization of Iron Bound to Transferrin by Vibrio parahaemolyticus

Contact Info

Product

Resources

About