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Background: Mycoplasma hyopneumoniae, the primary pathogen responsible for porcine enzootic pneumonia, reduces average daily weight gain and causes substantial economic losses to the pig industry worldwide. Vaccination is the most common strategy to control this disease but offers partial protection. Therefore, developing next‐generation vaccines by screening protective antigens is crucial. Objectives: The aim of this study was to evaluate the antibody response to 33 recombinant proteins in pigs naturally infected with M. hyopneumoniae. Methods: The genes encoding 33 (hypothetical) membrane proteins or secretory proteins were ligated into pGEX‐6P‐1, pGEX‐6P‐2, pGEX‐5X‐3 or pGEX‐4T‐3 vectors and transformed into Escherichia coli BL21(DE3) or E. coli XL‐1 Blue to construct recombinant bacteria and to express the recombinant proteins. The recombinant bacteria expressing the target proteins reacted with porcine convalescent sera and negative sera to screen immunodominant proteins by ELISA. Then, recombinant bacteria expressing immunodominant proteins were used to identify the discriminating immunodominant proteins that were recognised by convalescent sera nut not hyperimmune sera. Results: All recombinant bacteria could express the target recombinant proteins in soluble form. Twenty‐one proteins were shown to present immunodominant antigens, and four proteins were not recognised by convalescent sera. Moreover, six proteins were considered discriminating and reacted with convalescent sera but not with hyperimmune sera. Conclusions: The identified immunodominant proteins were antigenic and expressed during bacterial infection, suggesting that these proteins, especially those capable of discriminating between sera, can be used to identify protective antigens with the view to develop more effective vaccines against M. hyopneumoniae infection. [ABSTRACT FROM AUTHOR]

High external quantum efficiency (EQE) up to 25% has recently been reported from tetra(t‐butyl)rubrene (TBRb)‐based organic light‐emitting diodes (OLEDs), but its physical origin is still vague. Herein, using the featured responses of the evolution processes of electron‐hole pairs to an external magnetic field, an unreported high‐level reverse intersystem‐crossing (HL‐RISC) from upper‐level triplet to lowest singlet excitons (T2→S1) is observed when T2 is well confined in the active layer of pure TBRb. This HL‐RISC channel becomes stronger with lowering operational temperatures because it is not an endothermic process. Due to the larger separation distance of TBRb molecules with four tert‐butyl groups, the intersystem‐crossing (ISC) process of polaron pairs is stronger than the singlet fission (SF) process existing in pure TBRb, which is markedly different from the behaviors of excited states in pure rubrene (Rb) with negligible ISC and strong SF. More importantly, HL‐RISC is stronger in TBRb than in Rb‐doped systems, which is consistent with the higher EQE frequently reported from TBRb‐doped OLEDs. Thus, this work deepens the physical understanding of microscopic processes in typical organic multi‐functional semiconductors of TBRb or Rb and paves the way for fabricating further high‐efficiency yellow OLEDs. [ABSTRACT FROM AUTHOR]

Mycoplasma hyopneumoniae is the pathogen of porcine enzootic pneumonia (PEP). Due to difficulties in studying the pathogenesis of M. hyopneumoniae for blockage on the establishment of gene operation platform and immature animal model, mycoplasmologists still make progress in understanding the interaction between M. hyopneumoniae and host. In this paper, we review the adhesion and damage of M. hyopneumoniae to host cells, the inflammatory response and immune response of host stimulated by M. hyopneumoniae. Meanwhile, we propose research directions of the pathogenesis of M. hyopneumoniae in the future. This review can provide references for the follow-up study on the interaction between M. hyopneumoniae and host, and provide theoretical basis for effective vaccine and drug development.