Exact(1)
In low threshold mechanoreceptors (i.e. capsaicin-insensitive cells displaying RA currents) the toxin did not affect currents evoked by a 9 µm stimulus although at the higher stimulus intensity 2/5 neurons displayed toxin sensitivity.
Similar(59)
Furthermore, we show that specific selection of the displayed toxins by biopanning.
In addition, HNPs have been reported to display toxin-inactivating and immunomodulatory effects.
Using the system described here we have successfully displayed Cry3Aa toxin that is toxic to coleopteran insects (Additional file 1: Figure S1).
The toxicity of the virions Cry1Ac-M13 wanalyzedzed in bioassays by diet surface exposure showing that Cry1Ac-M13 was toxic to M. sexta larvae indicating that the display toxin retains its insecticidal activity (Fig. 2d).
Additionally, these effectors also display certain toxin domains, such as those pertaining to the eukaryotic Ub-systems that are not deployed in classical polymorphic toxin systems used in intraspecific conflict.
Fig. 3 a Western blot analysis of M13 phage particles displaying Cyt1Aa toxin prepared from E. coli cells harbouring the phagemid pCADS-Cyt1Aa.
Fig. 2 a Western blot analysis of 1011 M13 phages displaying Cry1Ac toxin prepared from E. coli cells harbouring the phagemids pCANTAB 5E-Cry1Ac (lane 2), pCAD-Cry1Ac (lane 3) or pCADS-Cry1Ac (lane 4).
With exceptions discussed in the preceding subsection, bacteria across most well-sampled ecosystems display polymorphic toxin systems.
Several toxins delivered via the PVC-SS displayed a putative toxin domain belonging to the OmpA superfamily of peptidoglycan-binding domains [ 171- 173] (e.g. gi: 171059731 from Leptothrix cholodnii; Figure 4C).
Together these results show that the display Cry1Ac toxin using the ssDsbA retains its receptor binding and toxicity features suggesting no structural constrains in the toxin displayed.
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