Outer membrane proteins induced under conditions of iron limitation in the marine fish pathogen Vibrio anguillarum 775.

1981 ◽  
Vol 31 (1) ◽  
pp. 223-227 ◽  
Author(s):  
J H Crosa ◽  
L L Hodges
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Marine Fish ◽  
Outer Membrane Proteins ◽  
Vibrio Anguillarum ◽  
Iron Limitation ◽  
Fish Pathogen

scholarly journals Siderophore production and outer membrane proteins of selectedVibrio vulnificusstrains under conditions of iron limitation

1986 ◽  
Vol 35 (2-3) ◽  
pp. 255-260 ◽  
Author(s):  
Anita C. Wright ◽  
Linda M. Simpson ◽  
Kathleen Richardson ◽  
David R. Maneval ◽  
James D. Oliver ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Siderophore Production ◽  
Iron Limitation

scholarly journals Two tonB Systems Function in Iron Transport in Vibrio anguillarum, but Only One Is Essential for Virulence

2004 ◽  
Vol 72 (12) ◽  
pp. 7326-7329 ◽  
Author(s):  
Michiel Stork ◽  
Manuela Di Lorenzo ◽  
Susana Mouriño ◽  
Carlos R. Osorio ◽  
Manuel L. Lemos ◽  
...  
Keyword(s):  
Marine Fish ◽  
Iron Transport ◽  
Vibrio Anguillarum ◽  
Iron Limitation ◽  
Fish Pathogen

ABSTRACT We have identified two functional tonB systems in the marine fish pathogen Vibrio anguillarum, tonB1 and tonB2. Each of the tonB genes is transcribed in an operon with the cognate exbB and exbD genes in response to iron limitation. Only tonB2 is essential for transport of ferric anguibactin and virulence.

scholarly journals Iron Uptake Mechanisms in the Fish Pathogen Tenacibaculum maritimum

2005 ◽  
Vol 71 (11) ◽  
pp. 6947-6953 ◽  
Author(s):  
Ruben Avendaño-Herrera ◽  
Alicia E. Toranzo ◽  
Jesús L. Romalde ◽  
Manuel L. Lemos ◽  
Beatriz Magariños
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Iron Uptake ◽  
Outer Membrane Proteins ◽  
Chelating Agent ◽  
Proteinase K ◽  
Fish Pathogen ◽  
Whole Cells ◽  
Iron Deficient ◽  
Uptake Mechanisms

ABSTRACT We present here the first evidence of the presence of iron uptake mechanisms in the bacterial fish pathogen Tenacibaculum maritimum. Representative strains of this species, with different serotypes and origins, were examined. All of them were able to grow in the presence of the chelating agent ethylenediamine-di- (o-hydroxyphenyl acetic acid) (EDDHA) and also produced siderophores. Cross-feeding assays suggest that the siderophores produced are closely related. In addition, all T. maritimum strains utilized transferrin, hemin, hemoglobin, and ferric ammonic citrate as iron sources when added to iron-deficient media. Whole cells of all T. maritimum strains, grown under iron-supplemented or iron-restricted conditions, were able to bind hemin, indicating the existence of constitutive binding components located at the T. maritimum cell surface. This was confirmed by the observation that isolated total and outer membrane proteins from all of the strains, regardless of the iron levels of the media, were able to bind hemin, with the outer membranes showing the strongest binding. proteinase K treatment of whole cells did not affect the hemin binding, indicating that, in addition to proteins, some protease-resistant components could also bind hemin. At least three outer membrane proteins were induced in iron-limiting conditions, and all strains, regardless of their serotype, showed a similar pattern of induced proteins. The results of the present study suggest that T. maritimum possesses at least two different systems of iron acquisition: one involving the synthesis of siderophores and another that allows the utilization of heme groups as iron sources by direct binding.

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