scholarly journals The genes that encode the gonococcal transferrin binding proteins, TbpB and TbpA, are differentially regulated by MisR under iron-replete and iron-depleted conditions

2016 ◽  
Vol 102 (1) ◽  
pp. 137-151 ◽  
Author(s):  
Justin L. Kandler ◽  
Rosuany Vélez Acevedo ◽  
Mary Kathryne Dickinson ◽  
Devin R. Cash ◽  
William M. Shafer ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Transferrin Binding Proteins

scholarly journals Transferrin Binding Proteins as a Means to Obtain Iron in Parasitic Protozoa

10.5772/48288 ◽  
2012 ◽  
Author(s):  
Magda Reyes-Lpez ◽  
Jess Serrano-Luna ◽  
Carolina Pia-Vzquez ◽  
Mireya de la Garz
Keyword(s):  
Binding Proteins ◽  
Parasitic Protozoa ◽  
Transferrin Binding Proteins

Methods for Manipulation of Transferrin-Binding Proteins

2003 ◽  
pp. 109-120 ◽  
Author(s):  
Leanne M. DeWinter ◽  
Anthony B. Schryvers
Keyword(s):  
Binding Proteins ◽  
Transferrin Binding Proteins

scholarly journals Gonococcal Genes Encoding Transferrin-Binding Proteins A and B Are Arranged in a Bicistronic Operon but Are Subject to Differential Expression

2001 ◽  
Vol 69 (10) ◽  
pp. 6336-6347 ◽  
Author(s):  
Chalinee Ronpirin ◽  
Ann E. Jerse ◽  
Cynthia Nau Cornelissen
Keyword(s):  
Binding Proteins ◽  
Iron Acquisition ◽  
Sole Source ◽  
Mrna Levels ◽  
Rt Pcr ◽  
Upstream Promoter ◽  
Genes Encoding ◽  
Transferrin Binding Proteins ◽  
Iron Binding Proteins ◽  
Fusion Analysis

ABSTRACT Neisseria gonorrhoeae is capable of utilizing host iron-binding proteins, such as transferrin, lactoferrin, and hemoglobin, as the sole source of iron. The receptor involved in transferrin iron acquisition is composed of two distinct transferrin-binding proteins, TbpA and TbpB. The genes that encode these proteins are linked on the chromosome in the ordertbpB-tbpA but are separated by an inverted repeat of unknown function. In this study, we sought to understand the transcriptional organization and regulation of thetbp genes, using a combination of lacZtranscriptional fusion analysis and reverse transcriptase PCR (RT-PCR). First, we demonstrated that tbpB and tbpAare cotranscribed and coregulated from the common upstream promoter that precedes tbpB. Using β-galactosidase activity as a surrogate for tbp-specific transcription, we found that tbpB-specific transcripts were more prevalent thantbpA-specific transcripts after 2 h of growth under iron stress conditions. We confirmed the results obtained by fusion analysis by using RT-PCR applied to native RNA isolated from wild-type gonococci. Three different varieties of RT-PCR were employed: relative, competitive, and real time quantitative. The results of all analyses indicated that tbpB-specific transcripts were approximately twofold more prevalent than tbpA-specific transcripts at steady state. In iron-stressed cultures, the ratio oftbpB- to tbpA-specific message was approximately 2; however, in iron-replete cultures, this ratio dropped to 1. Using these techniques, we also quantitated the effects of iron, external pH, and presence of ligand on tbp mRNA levels.

Transferrin-mediated iron acquisition by pathogenic Neisseria

2002 ◽  
Vol 30 (4) ◽  
pp. 705-707 ◽  
Author(s):  
R. W. Evans ◽  
J. S. Oakhill
Keyword(s):  
Bacterial Cell ◽  
Iron Uptake ◽  
Binding Proteins ◽  
Current Knowledge ◽  
Iron Acquisition ◽  
Direct Interaction ◽  
Acquisition System ◽  
Uptake System ◽  
Short Account ◽  
Transferrin Binding Proteins

The pathogenic Neisseria have a siderophore-independent iron-uptake system reliant on a direct interaction between the bacterial cell and transferrin. In the meningococcus this uptake system is dependent on two surface-exposed transferrin-binding proteins. This short account will review our current knowledge of the transferrin-mediated iron-acquisition system of pathogenic Neisseria.

Transferrin-binding proteins isolated from Neisseria meningitidis elicit protective and bactericidal antibodies in laboratory animals

Vaccine ◽  
1993 ◽  
Vol 11 (12) ◽  
pp. 1214-1220 ◽  
Author(s):  
B. Danve ◽  
L. Lissolo ◽  
M. Mignon ◽  
P. Dumas ◽  
S. Colombani ◽  
...  
Keyword(s):  
Neisseria Meningitidis ◽  
Binding Proteins ◽  
Laboratory Animals ◽  
Transferrin Binding Proteins

Optimization of membrane isolation and transferrin-binding proteins solubilization from Neisseria meningitidis cells

1998 ◽  
Vol 31 (3) ◽  
pp. 151-157
Author(s):  
Beatriz Echeverrı́a ◽  
José Antonio Gómez ◽  
Ernesto Hernández ◽  
Marı́a Teresa Criado ◽  
Carlos Ferreirós
Keyword(s):  
Neisseria Meningitidis ◽  
Binding Proteins ◽  
Membrane Isolation ◽  
Transferrin Binding Proteins

scholarly journals Analysis of the human Ig isotype response to individual transferrin binding proteins A and B from Neisseria meningitidis

2006 ◽  
Vol 19 (2) ◽  
pp. 159-167 ◽  
Author(s):  
Alison S Johnson ◽  
Andrew R Gorringe ◽  
Andrew J Fox ◽  
Ray Borrow ◽  
Andrew Robinson
Keyword(s):  
Neisseria Meningitidis ◽  
Binding Proteins ◽  
Transferrin Binding Proteins
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