scholarly journals Epitope mapping and the kinetic signatures of antibody binding to the Mycoplasma genitalium MgpB adhesin protein

Author(s):  
Margaret Lunn
2016 ◽  
Vol 138 (6) ◽  
pp. 1728-1730 ◽  
Author(s):  
Christian S. Hansen ◽  
Martin Dufva ◽  
Katrine L. Bøgh ◽  
Eric Sullivan ◽  
Jigar Patel ◽  
...  

1996 ◽  
Vol 26 (6) ◽  
pp. 514-521 ◽  
Author(s):  
J. G. ROUTSIAS ◽  
A. G. TZIOUFAS ◽  
M. SAKARELLOS-DAITSIOTIS ◽  
C. SAKARELLOS ◽  
H. M. MOUTSOPOULOS

2017 ◽  
Vol 13 (12) ◽  
pp. 2953-2966 ◽  
Author(s):  
Daniel R. Ripoll ◽  
Daniel A. J. Mitchell ◽  
Lesley C. Dupuy ◽  
Anders Wallqvist ◽  
Connie Schmaljohn ◽  
...  

2006 ◽  
Vol 74 (7) ◽  
pp. 3715-3726 ◽  
Author(s):  
Stefanie L. Iverson-Cabral ◽  
Sabina G. Astete ◽  
Craig R. Cohen ◽  
Eduardo P. C. Rocha ◽  
Patricia A. Totten

ABSTRACT Mycoplasma genitalium is associated with reproductive tract disease in women and may persist in the lower genital tract for months, potentially increasing the risk of upper tract infection and transmission to uninfected partners. Despite its exceptionally small genome (580 kb), approximately 4% is composed of repeated elements known as MgPar sequences (MgPa repeats) based on their homology to the mgpB gene that encodes the immunodominant MgPa adhesin protein. The presence of these MgPar sequences, as well as mgpB variability between M. genitalium strains, suggests that mgpB and MgPar sequences recombine to produce variant MgPa proteins. To examine the extent and generation of diversity within single strains of the organism, we examined mgpB variation within M. genitalium strain G-37 and observed sequence heterogeneity that could be explained by recombination between the mgpB expression site and putative donor MgPar sequences. Similarly, we analyzed mgpB sequences from cervical specimens from a persistently infected woman (21 months) and identified 17 different mgpB variants within a single infecting M. genitalium strain, confirming that mgpB heterogeneity occurs over the course of a natural infection. These observations support the hypothesis that recombination occurs between the mgpB gene and MgPar sequences and that the resulting antigenically distinct MgPa variants may contribute to immune evasion and persistence of infection.


2015 ◽  
Vol 113 (02) ◽  
pp. 396-405 ◽  
Author(s):  
Joerg Kahle ◽  
Aleksander Orlowski ◽  
Diana Stichel ◽  
Karin Becker-Peters ◽  
Ali Kabiri ◽  
...  

SummaryThe most serious complication in today’s treatment of congenital haemophilia A is the development of neutralising antibodies (inhibitors) against factor VIII (FVIII). Although FVIII inhibitors can be eliminated by immune tolerance induction (ITI) based on repeated administration of high doses of FVIII, 20–30% of patients fail to become tolerant. Persistence of FVIII inhibitors is associated with increased morbidity and mortality. Data from recent studies provide evidence for a potential association between ITI outcome and epitope specificity of FVIII inhibitors. Nevertheless the determination of epitopes and their clinical relevance has not yet been established. In this study a general strategy for the identification of anti-FVIII antibody epitopes in haemophilia A patient plasma was to be demonstrated. Phage-displayed peptide libraries were screened against anti-FVIII antibodies to isolate specific peptides. Peptide specificity was confirmed by FVIII-sensitive ELISA binding. Peptide residues essential for antibody binding were identified by mutational analysis and epitopes were predicted via FVIII homology search. The proposed mapping strategy was validated for the monoclonal murine antibody (mAb) 2–76. Binding studies with FVIII variants confirmed the location of the predicted epitope at the level of individual amino acids. In addition, anti-FVIII antibody-specific peptide ligands were selected for 10 haemophilia A patients with FVIII inhibitors. Detailed epitope mapping for three of them showed binding sites on the A2, A3 and C2 domains. Precise epitope mapping of anti-FVIII antibodies using antibody-specific peptide ligands can be a useful approach to identify antigenic sites on FVIII.


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