2018
DOI: 10.3389/fmicb.2018.02915
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Lipid-Modified Azurin of Neisseria gonorrhoeae Is Not Surface Exposed and Does Not Interact With the Nitrite Reductase AniA

Abstract: Lipid-modified cupredoxin azurin (Laz) is involved in electron transport in Neisseria and proposed to act as an electron donor to the surface-displayed nitrite reductase AniA. We identified Laz in Neisseria gonorrhoeae cell envelopes and naturally elaborated membrane vesicles in proteomic investigations focused on discovering new vaccine and therapeutic targets for this increasingly difficult to treat pathogen. Its surface exposure in N. meningitidis suggested Laz could be a vaccine candidate for N. gonorrhoea… Show more

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Cited by 4 publications
(2 citation statements)
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References 78 publications
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“…The redox partner of this enzyme is still unknown, and it has been shown not to be the lipid-modified azurin from the same organism [ 36 ], though this protein is also bound to the outer membrane and it is the redox partner of another outer membrane-attached enzyme, the bacterial peroxidase [ 37 , 38 ].…”
Section: Introductionmentioning
confidence: 99%
“…The redox partner of this enzyme is still unknown, and it has been shown not to be the lipid-modified azurin from the same organism [ 36 ], though this protein is also bound to the outer membrane and it is the redox partner of another outer membrane-attached enzyme, the bacterial peroxidase [ 37 , 38 ].…”
Section: Introductionmentioning
confidence: 99%
“…It is described as an homotrimer and is found in the periplasm of N gonorrhoeae , anchored to the outer membrane by a palmitate bound to a cysteine residue [23]. The redox partner of this enzyme is still not known and was shown not to be the lipid-modified azurin from the same organism [24].…”
Section: Introductionmentioning
confidence: 99%