Flexible transparent conductors are an enabling component for large-area flexible displays, wearable electronics, and implantable medical sensors that can wrap around and move with the body. However, conventional conductive materials decay quickly under tensile strain, posing a significant hurdle for functional flexible devices. Here, we show that high electrical conductivity, mechanical stretchability, and optical transparency can be simultaneously attained by compositing long metallic double-walled carbon nanotubes with a polydimethylsiloxane substrate. When stretched to 100% tensile strain, thin films incorporating these long nanotubes (≈3.2 µm on average) achieve a record high conductivity of 3316 S cm at 100% tensile strain and 85% optical transmittance, which is 194 times higher than that of short nanotube controls (≈0.8 µm on average). Moreover, the high conductivity can withstand more than 1000 repeated stretch-release cycles (switching between 100% and 0% strain) with a retention approaching 96%, whereas the short nanotube controls exhibit only 10%. Mechanistic studies reveal that long tubes can bridge the microscale gaps generated during stretching, thereby maintaining high electrical conductivity. When mounted on human joints, this elastic transparent conductor can accommodate large motions to provide stable, high current output. These results point to transparent conductors capable of attaining high electrical conductivity and optical transmittance under mechanical strain to allow large shape changes that may take place in the operation and use of flexible electronics.
Background The thrombospondin-related anonymous protein (TRAP) was first discovered in the sporozoite of Plasmodium falciparum and TRAP family proteins are secreted by micronemes and transported to the parasite surface to participate in the invasion process. Various TRAP proteins have been identified in apicomplexan protozoans, but there have been few reports about TRAP proteins in Babesia orientalis . Methods The functional domain of TRAP2 in B. orientalis was cloned, sequenced, characterized and compared to the TRAP sequences of related apicomplexan parasites. The functional domain of BoTRAP2 was truncated, named BoTRAP2-1, and then cloned into the pET-28a expression vector. Rabbit anti-rBoTRAP2-1 polyclonal antibody was produced by immunizing three rabbits. Western blot analysis was used to identify the native form and immunogenicity of BoTRAP2. The localization of BoTRAP2 was identified by indirect fluorescence assay (IFA). Results The amplified genes of BoTRAP2 are 2817 bp in length, encoding a functional domain of about 938 aa with two vWFA domains, one TSP domain and one transmembrane domain. The amino acid sequence of BoTRAP2 has a high similarity with that of B. bovis and B. gibsoni . The predicted tertiary structure of truncated BoTRAP2-1 confirmed that BoTRAP2 contains two vWFA domains and a TSP domain, the main functional areas of the protein. The native BoTRAP2 was identified from B. orientalis lysate by using rabbit polyclonal anti-rBoTRAP2-1. A band corresponding to rBoTRAP2-1 was detected by reaction with serum from a B. orientalis -infected water buffalo, indicating that the protein has a high immunogenicity. IFA showed that BoTRAP2 is mainly localized on the apical end of parasites by rabbit anti-rBoTRAP2-1 polyclonal serum. Conclusions The rBoTRAP2 could differentiate serum from B. orientalis -infected water buffalo and normal water buffalo, implicating that BoTRAP2 has high immunogenicity and could serve as a candidate antigen for diagnosis of B. orientalis infection in buffalo. Electronic supplementary material The online version of this article (10.1186/s13071-019-3457-0) contains supplementary material, which is available to authorized users.
BackgroundThe thrombospondin-related anonymous protein (TRAP) family, a kind of transmembrane protein, is widely distributed with a conserved feature of structure in all apicomplexan parasites and plays a crucial role in the gliding motility and survival of parasites.MethodsThe Babesia orientalis TRAP1 gene (BoTRAP1) was truncated and cloned into a pET-42b expression vector and expressed as a GST-tag fusion protein with a TEV protease site. Rabbit anti-rBoTRAP1 antibody was produced and purified using a protein A chromatography column. Western blot analysis was performed to identify the native protein of BoTRAP1 and differentiate B. orientalis-infected positive from negative serum samples. The localization of BoTRAP1 on merozoites was identified by the indirect florescent antibody test (IFAT).ResultsThe partial sequence of the TRAP1 gene was cloned from B. orientalis cDNA and identified to contain a von Willebrand factor A (vWFA) region and a thrombospondin type-1 (TSP-1) domain; it had a length of 762 bp, encoding a polypeptide of 254 amino acid residues with a predicted size of 28.2 kDa. The partial sequence was cloned into a pET-42b expression vector and expressed in E. coli as a GST fusion protein. Western blot indicated that rBoTRAP1 has a high immunogenicity and can differentiate B. orientalis-infected positive and negative serum samples collected from water buffaloes. IFAT showed that BoTRAP1 is mainly localized on the apical end of intracellular parasites by using polyclonal antibodies (PcAb) against rBoTRAP1. Meanwhile, the PcAb test also identified the native BoTRAP1 as a ~65 kDa band from B. orientalis lysates. The predicted 3D structure of BoTRAP1 contains a metalion-dependent adhesion site (MIDAS), which could be important for interaction with ligand on the surface of the host cells.ConclusionsLike all known protozoa, B. orientalis has a TRAP family, comprising TRAP1, TRAP2, TRAP3 and TRAP4. The newly identified and characterized BoTRAP1 may play a key role in the invasion of B. orientalis into water buffalo erythrocytes.
The tick-and transfusion-transmitted human pathogen Babesia microti infects host erythrocytes to cause the pathologic symptoms associated with human babesiosis, an emerging disease with worldwide distribution and potentially fatal clinical outcome. Drugs currently recommended for the treatment of babesiosis are associated with a high failure rate and significant adverse events, highlighting the urgent need for more-effective and safer babesiosis therapies. Unlike other apicomplexan parasites, B. microti lacks a canonical lactate dehydrogenase (LDH) but instead expresses a unique enzyme, B. microti LDH (BmLDH), acquired through evolution by horizontal transfer from a mammalian host. Here, we report the crystal structures of BmLDH in apo state and ternary complex (enzyme-NADH-oxamate) solved at 2.79 and 1.89Å. Analysis of these structures reveals that upon binding to the coenzyme and substrate, the active pocket of BmLDH undergoes a major conformational change from an opened and disordered to a closed and stabilized state. Biochemical assays using wild-type and mutant B. microti and human LDHs identified Arg99 as a critical residue for the catalytic activity of BmLDH but not its human counterpart. Interestingly, mutation of Arg99 to Ala had no impact on the overall structure and affinity of BmLDH to NADH but dramatically altered the closure of the enzyme's active pocket. Together, these structural and biochemical data highlight significant differences between B. microti and human LDH enzymes and suggest that BmLDH could be a suitable target for the development of selective antibabesial inhibitors.
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