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Overall, these data illustrate that δ-toxin directly interacts with, and binds to, host AMPs.
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Overall, we show here that δ-toxin is able to bind to host AMPs.
LL-37 binds to host DNA [16].
These traps are formed when AMPs bind to host DNA, histones and proteases to form a matrix that entraps and kills invading pathogens [22].
Borreliae are obligatorily bound to host organisms for survival.
Since previous studies suggest that AMPs form heterodimeric and homodimeric complexes [21], and because we found that δ-toxin colocalizes with LL-37 in NETs, we hypothesized that δ-toxin physically binds to the host derived AMPs.
To determine the ability of the host AMPs to interact with δ-toxin, the peptide was incubated with host AMPs and tryptophan emission was monitored upon excitation at 290 nm (Figure 4b and 4c).
Microorganisms which bind to the host cell targets promoting host responses cause these diseases [1, 2].
They bind to the host cell membrane and play important roles in bacteria-host interactions [ 33].
Due to the spectroscopic silence of the host AMPs, a maximal tryptophan emission shift in δ-toxin during incubation with a host AMP would signify an interaction with and structural change of δ-toxin.
Moreover, host AMPs have been shown to act synergistically with an antimicrobial peptide produced by L. lactis to inhibit E. coli [18].
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