The PBPs involved in bacterial iron uptake have historically been classified as either unchelated iron binders or chelated iron binders (i.e., iron-siderophore complex binders).
Detailed analysis performed in our previous study [ 15] indicates that HA is comparable, in its solubility effect, to the best known classical complex binders of [Ca2+] or [C2O42−] ions in urine, that is, [Mg2+] and citrate anions.
The third cluster exhibited strong binding only in human sperm consisted of Gal-binder (MAL II), complex-binder (PHA-L, PHA-E + L, PHA-E), Sia-binder (SNA) and one unknown specific lectin (PHA-P).
The two SEB binders along with the BoNT/A complex toxoid binder, P4BF7-3, had no formation of inter-loop disulfide bonds and shared a conserved W31 within CDR1, which are major features of type 3 NAR V originally defined as appearing only in juvenile nurse sharks less than one year old [ 5, 18].
This is also in line with previous findings that link dorsal temporal brain areas including HG and planum temporale with the analysis of auditory features of complex sounds (Binder et al. 1996; Wessinger et al. 2001; Hall et al. 2002, 2003; Seifritz et al. 2002).
However, the multiple-peak phenomenon observed in the BYET stress-strain curves of some of the complex modified binders makes it very difficult to clearly identify the failure parameters.
The two BoNT/A complex toxoid binders, P4BH8 and P4BF7-3, varied significantly in amino acid composition within the four hypervariable regions, suggesting they target different epitopes.
One of the BoNT/A complex toxoid binders (P4BF7-3) was fairly specific to BoNT complex toxoid subtypes, but the other (P4BH8) showed significant non-specific binding to ricin and CT (Figs. 3B and 3C).
Both BoNT/A complex toxoid binders retained a substantial amount (60%–80%) of the original binding activity after being heated for 60 min at 85°C, while non-specific binding was actually reduced over the same period (Figs 4D and 4E).
One of the BoNT/A complex toxoid binders, P4BH8, is an atypical type 1 NAR V that lacks Cys residues in FR2 and FR4 but contains two CDR3 Cys residues, which allows the formation of an intra-loop disulfide bridge to stabilize CDR conformation.
