Conservation of Ni-binding ligands was also analyzed for each Ni-dependent protein and those lacking most of the ligands were discarded.
CFH-binding to borreliae was also analyzed for cell lysates derived from CRASP-3 and CRASP-5 expressing transformants and the non-expressing control strains G1 and G1/pKFSS1.
The chloride binding capacity of RAC was also analyzed.
The relative location of the binding region with respect to the gene was also analyzed, and the binding regions were classified into three categories: upstream from the gene (distinguishing between far upstream and close upstream), internal to the gene (close to the 5′ or the 3′ end of the gene), and downstream from the gene (Table 1 and Additional file 2: Table S1).
Dissociation from a control sequence, a 24-mer DNA duplex with no known tetraintercalator binding site (5′-CATTTAACAACATGTTGTTGGCTC-3′), was also analyzed.
To determine if the hits isolated only once in the library screen were of comparable quality or inferior to those isolated multiple times, their binding to the anti-ADP3 antibodies was also analyzed using fluorescence polarization.
Binding capacity of EDAvidin to biotinylated proteins was also analyzed by surface plasmon resonance (SPR) using ProteOn XPR36 (Bio-Rad, Hercules, CA, USA) optical biosensor.
Another ESAT6 binding peptide, SL3, from our previous studies [ 16] was also analyzed for its effects on mycobacterial growth during this study (unpublished results).
Serum was also analyzed for testosterone, estradiol, sex hormone-binding globulin (SHBG), inhibin B, luteinizing hormone (LH), and follicle-stimulating hormone (FSH).
Plasma was also analyzed for LPS, interleukin 6 (IL-6) cytokine and acute phase proteins: serum amyloid A (SAA), LPS binding protein (LBP) and haptoglobin (Hp).
