Objective:To explore the application effectiveness of Artificial Intelligence Generated Content(AIGC)in immuno-logy education and optimize teaching models to enhance students'clinical thinking and self-directed learning abilities.Methods:A questionnaire survey was conducted to analyze the current application status of AIGC among 105 university teachers.Taking"TypeⅠHypersensitivity"as an example,integrating AI tools to generate dynamic case scenarios and multimodal resources.Teaching effective-ness was evaluated through classroom practices and student questionnaires.Results:88.32%of teachers recognized AIGC's role in im-proving preparation efficiency,and 61.54%of students reported significantly improved learning outcomes.However,71.43%of teach-ers expressed concerns about increased student dependency,and 55.84%of teachers emphasized challenges in content quality control.Conclusion:AIGC effectively enhances teaching interactivity and personalized learning.Future efforts should focus on optimizing con-tent authority,establishing ethical guidelines,and promoting the development of human-AI collaborative educational models.

Influenza is a major public health problem worldwide,resulting in millions of hospitalizations each year.In addi-tion to vaccination and antiviral drugs against influenza,monoclonal antibody therapy is a promising treatment method because of its cross-reactivity and targeting.Widely reactive monoclonal antibodies can bind and neutralize multiple subtypes of influenza A virus,and also show good protective effect on infected mice,showing high potential in the prevention and treatment of influenza.In this review,we briefly review the recent research progress of broad-spectrum monoclonal antibodies targeting HA and NA,two important surface glycoproteins of influenza A virus.

Influenza is a major public health problem worldwide,resulting in millions of hospitalizations each year.In addi-tion to vaccination and antiviral drugs against influenza,monoclonal antibody therapy is a promising treatment method because of its cross-reactivity and targeting.Widely reactive monoclonal antibodies can bind and neutralize multiple subtypes of influenza A virus,and also show good protective effect on infected mice,showing high potential in the prevention and treatment of influenza.In this review,we briefly review the recent research progress of broad-spectrum monoclonal antibodies targeting HA and NA,two important surface glycoproteins of influenza A virus.

Objective:To explore the application effectiveness of Artificial Intelligence Generated Content(AIGC)in immuno-logy education and optimize teaching models to enhance students'clinical thinking and self-directed learning abilities.Methods:A questionnaire survey was conducted to analyze the current application status of AIGC among 105 university teachers.Taking"TypeⅠHypersensitivity"as an example,integrating AI tools to generate dynamic case scenarios and multimodal resources.Teaching effective-ness was evaluated through classroom practices and student questionnaires.Results:88.32%of teachers recognized AIGC's role in im-proving preparation efficiency,and 61.54%of students reported significantly improved learning outcomes.However,71.43%of teach-ers expressed concerns about increased student dependency,and 55.84%of teachers emphasized challenges in content quality control.Conclusion:AIGC effectively enhances teaching interactivity and personalized learning.Future efforts should focus on optimizing con-tent authority,establishing ethical guidelines,and promoting the development of human-AI collaborative educational models.

Objective:To establish an antibody expression system to reduce the antibody-dependent enhancement (ADE) effect of target antibody.Methods:Site-directed mutagenesis was used to mutate the 234 and 235 sites of the Fc region of the mammalian cell antibody expression vector-L234A and L235A to establish the antibody expression vector pFRT-IgG1κ-FcM. An antibody Wt-WNV with significant ADE effect obtained in previous work was selected and expressed by the pFRT-IgG1κ-FcM system to obtain mutant antibody FcM-WNV. The binding ability of FcM-WNV to target antigen West Nile virus envelope protein-DⅢ (WNV E-DⅢ) was detected by ELISA, and the its binding ability to human high-affinity IgG Fc receptor hFcγRⅠ (hCD64 ) was analyzed by flow cytometry. The neutralizing activity of FcM-WNV in vitro was detected by pseudovirus infection of host cells (BHK21 and K562). Results:The expression levels of FcM-WNV and Wt-WNV were comparable, and FcM-WNV could recognize and bind to WNVE-DIII in a concentration-dependent manner. Compared with Wt-WNV, the binding ability of FcM-WNV to hCD64 was significantly weakened, showing a significant decrease in fluorescence intensity. Consistent with the previous experimental results, Wt-WNV at a concentration of 5 μg/ml significantly enhanced the infection of K562 by WNV pseudovirus, while FcM-WNV at a concentration of 5 μg/ml could effectively block pseudovirus infection in both K562 and BHK21 cells.Conclusions:The established antibody expression system can effectively reduce the ADE effect of the target antibody.

Objective:To establish an in vivo infection model of H5N1 pseudovirus and to detect the neutralizing activity of FHA3 antibody using this model. Methods:Based on the sequence information of hemagglutinin (HA) and neuraminidase (NA) of A/Anhui/1/2005/H5N1 strain, two recombinant plasmids of pcDNA3.1-HA5 and pcDNA3.1-NA1 were constructed. The two plasmids and plasmid pNL4-3.Luc.R-E- were co-transfected into 293T cells to prepare H5N1 pseudovirus supernatant. The morphology of pseudovirus particles in the supernatant was observed by electron microscopy. MDCK cells were infected with the pseudovirus supernatant and the virus titer was detected. BALB/c mice were injected with the pseudovirus supernatant by intraperitoneal injection and subjected to bioluminescence imaging at 2, 5, 8, and 12 d after infection to detect the pseudovirus infection in vivo. The functional activity of FHA3 antibody in vivo was evaluated using the established mouse infection model. Results:The recombinant plasmids pcDNA3.1-HA5 and pcDNA3.1-NA1 were correctly constructed and could be used to prepare pseudovirus supernatants of high titer by co-transfecting 293T cells with the plasmid pNL4-3.Luc.R-E-. The virus particles were round under electron microscope. H5N1 pseudovirus-infected mice exhibits strong fluorescence signals, which were attenuated by FHA3 treatment before challenge.Conclusions:The in vivo infection model of H5N1 pseudovirus was successfully constructed and FHA3 antibody was proved to be protective against the pseudovirus infection.

Flaviviruses are a class of positive-strand RNA viruses mainly transmitted by arthropods, which can cause high mortality and morbidity worldwide. At present, there is no specific therapy. Therapeutic antibodies bring hope for the treatment of flavivirus infection, but the antibody-dependent enhancement (ADE) effect induced by flavivirus infection can lead to disease progression. The ideal therapeutic antibodies against flaviviruses should not only treat flavivirus infection, but also avoid the harm caused by ADE. Therefore, researchers have optimized some of the antibodies to seek the best therapeutic antibodies. This review briefly described the research progress and mechanism of therapeutic antibodies against flaviviruses as well as some strategies to reduce the ADE effect induced by the therapeutic antibodies.

Neutralizing monoclonal antibodies against dengue virus cross-react with other flaviviruses due to the sequence homology between them, such as the antibodies targeting envelope protein and non-structural protein 1. Apart from exerting protective effects in infected animals, cross-neutralizing antibodies could also cause antibody-dependent enhancement (ADE) in vivo. This review summarized the progress in cross-reactivity of neutralizing antibodies against dengue virus.

Objective:To prepare and identify a broad-spectrum antibody FHA3 targeting influenza A virus hemagglutinin (HA).Methods:According to the single-chain antibody fragment (scFv) sequence, the heavy chain (VH) and light chain (VL) variable regions of FHA3 were amplified by PCR and a recombinant plasmid pFRT-IgG1κ-FHA3 was constructed by linking the expression vector pFRT-IgG1κ. FHA3 was expressed in the ExpiCHO system and purified by affinity purification. The binding activity of FHA3 to influenza A virus HA was detected by ELISA. The neutralizing activity of FHA3 was detected in vitro by infecting host cells with pseudovirus. Results:SDS-PAGE showed that high-purity FHA3 was obtained. FHA3 could bind to H1N1 HA, H2N2 HA, H3N2 HA, H5N1 HA, H7N9 HA and H9N2 HA in a concentration-dependent manner. FHA3 had good neutralizing activity in vitro that was it could effectively block the invasion of H5N1 and H7N9 pseudoviruses into target cells at a low concentration of 5 μg/ml and H1N1 pseudovirus at 0.012 5 μg/ml. Conclusions:A broad spectrum antibody targeting HA protein of influenza A virus with neutralizing activity in vitro was obtained.

Objective:To prepare and identify a functional antibody FNA1 targeting the neuraminidase (NA) of influenza A virus N1 subtype.Methods:According to single-chain antibody fragment (scFv) sequence, the heavy chain and light chain variable region sequences of FNA1 were synthesized, and the recombinant expression plasmid pFRT-IgG1κ-FNA1 was constructed by linking the expression vector pFRT-IgG1κ. The FNA1 antibody was expressed in ExpiCHO cells and purified using affinity purification technique. The binding ability of FNA1 to the target proteins, influenza A virus N1 subtype NA antigens, was detected by ELISA. Flow cytometry was performed to analyze the binding ability of FNA1 to the NA antigens expressed on the surface of cell membrane. The in vitro activity of FNA1 against NA was evaluated by infecting 293T cells with pseudovirus. Results:Protein electrophoresis showed that FNA1 with high purity was obtained. FNA1 specifically recognized and bound to N1 subtype NA antigens in a concentration-dependent manner. FNA1 could effectively block NA activity by binding to N1 subtype NA protein expressed on the surface of cell membrane, thus inhibiting the release of packaged pseudovirus from cell surface and further inhibiting target cell infection.Conclusions:An antibody FNA1 targeting influenza A virus N1 subtype NA with in vitro functional activity was obtained.