Asia Pacific Association of Allergy Asthma and Clinical Immunology White Paper 2020 on climate change, air pollution, and biodiversity in Asia-Pacific and impact on allergic diseases
Ruby PAWANKAR; Jiu-Yao WANG; I-Jen WANG; Francis THIEN; Yoon-Seok CHANG; Amir-Hamzah-Abdul LATIFF; Takao FUJISAWA; Luo ZHANG; Bernard-Yu-Hor THONG; Pantipa CHATCHATEE; Ting-Fan LEUNG; Wasu KAMCHAISATIAN; Iris RENGGANIS; Ho-Joo YOON; Sonomjamts MUNKHBAYARLAKH; Marysia-T. RECTO; Anne-Goh-Eng NEO; Duy LE-PHAM; Le-Thi-Tuyet LAN; Janet-Mary DAVIES; Jae-Won OH.
Asia Pacific Allergy ; (4): 11-2020.
Air pollution, climate change, and reduced biodiversity are major threats to human health with detrimental effects on a variety of chronic noncommunicable diseases in particular respiratory and cardiovascular diseases. The extent of air pollution both outdoor and indoor air pollution and climate change including global warming is increasing-to alarming proportions particularly in the developing world especially rapidly industrializing countries worldwide. In recent years, Asia has experienced rapid economic growth and a deteriorating environment and increase in allergic diseases to epidemic proportions. Air pollutant levels in many Asian countries especially in China and India are substantially higher than are those in developed countries. Moreover, industrial, traffic-related, and household biomass combustion, indoor pollutants from chemicals and tobacco are major sources of air pollutants, with increasing burden on respiratory allergies. Here we highlight the major components of outdoor and indoor air pollutants and their impacts on respiratory allergies associated with asthma and allergic rhinitis in the Asia-Pacific region. With Asia-Pacific comprising more than half of the world's population there is an urgent need to increase public awareness, highlight targets for interventions, public advocacy and a call to action to policy makers to implement policy changes towards reducing air pollution with interventions at a population-based level.
Administrative Personnel , Air Pollutants , Air Pollution , Air Pollution, Indoor , Allergy and Immunology , Asia , Asian Continental Ancestry Group , Asthma , Biodiversity , Biomass , Cardiovascular Diseases , China , Climate Change , Climate , Consumer Advocacy , Developed Countries , Economic Development , Family Characteristics , Global Warming , Humans , Hypersensitivity , India , Rhinitis, Allergic , Tobacco
Progress in shark single-domain antibody / 生物工程学报
Xing LIU; Qi CHEN.
Monoclonal antibody (mAb) is an important biological macromolecule and widely used in immune detection, in vitro diagnostics, and drug discovery. However, the inherent properties of mAb restrict its further development, such as high molecular weight and complex structure. Therefore, there is an urgent need to develop alternatives for mAb. Various types of miniaturized antibodies have been developed, among which the variable domain of immunoglobulin new antigen receptor (VNAR) is very attractive. The shark single-domain antibody, also known as shark VNAR, is an antigen-binding domain obtained by genetic engineering technology based on the immunoglobulin new antigen receptor (IgNAR) that naturally exists in selachimorpha. It has a molecular weight of 12 kDa, which is the smallest antigen-binding domain found in the known vertebrates at present. Compared with mAb, the shark VNAR exhibits various superiorities, such as low molecular weight, high affinity, tolerance to the harsh environment, good water solubility, strong tissue penetration, and recognition of the hidden epitopes. It has attracted wide attention in the fields of immunochemical reagents and drug discovery. In this review, various aspects of shark VNAR are elaborated, including the structural and functional characteristics, generating and humanization techniques, affinity maturation strategies, application fields, advantages and disadvantages, and prospects.
Animals , Antibodies, Monoclonal , Allergy and Immunology , Antibodies, Monoclonal, Humanized , Allergy and Immunology , Antigens , Epitopes , Metabolism , Protein Domains , Allergy and Immunology , Receptors, Antigen , Chemistry , Allergy and Immunology , Sharks
Formation of FADD amyloid fiber and its role in immune signaling in Drosophila melanogaster / 生物工程学报
Xinyi WANG; Xiaoyi XIAO; Chang SUN; Fei WANG.
In this research, we studied the formation of Drosophila melanogaster FADD (Fas-associated death domain-containing protein) amyloid fiber and its influence on signal transduction in IMD (Immune deficiency) signaling pathway to better understand the regulation mechanism of Drosophila innate immune signaling pathway, which will provide reference for the immune regulation in other species. First, we purified dFADD protein expressed in Escherichia coli and performed Sulfur flavin T binding and transmission electron microscopy to identify the dFADD amyloid fibers formed in vitro. Then we investigated the formation of dFADD polymers in S2 cells using SDD-AGE and confocal microscope. We also constructed dFADD mutants to find out which domain is essential to fiber formation and its effect on IMD signal transduction. Our results revealed that dFADD could be polymerized to form amyloid fiber polymers in vitro and inside the cells. Formation of fibers relies on DED (Death-effector domain) domain of dFADD, since DED domain-deleted mutant existed as a monomer. Dual luciferase reporter assay showed that intact DED domain was required for the induction of downstream antimicrobial peptides, indicating that fiber formation was the key to IMD signal transduction. Our study revealed the role of dFADD in mediating the cascade between IMD and Dredd in the IMD signaling pathway by forming amyloid fibers, suggesting an evolutionarily conserved regulatory mechanism of innate immune signaling pathway.
Animals , Drosophila Proteins , Allergy and Immunology , Drosophila melanogaster , Allergy and Immunology , Fas-Associated Death Domain Protein , Allergy and Immunology , Immunity, Innate , Allergy and Immunology , Signal Transduction
Effects of different signal peptides on the secretion of human-mouse chimeric CMV-IgM / 生物工程学报
Yamin CUI; Xiaoping TIAN; Qiaohui ZHAO; Guilin LI.
In order to prepare human-mouse chimeric cytomegalovirus-immunoglobulin M (CMV-IgM) in vitro and study the effects of different signal peptides on the secretion of CMV-IgM, genes were amplified from hybridoma cell line using RLM-RACE to construct the expression vector of chimeric CMV-IgM. Then, the signal peptide of SigF itself was replaced by five different secreted signal peptides (SigA-SigE) by PCR method, and the CHO cell was chosen as host cell for in vitro expression. SDS-PAGE, SEC-HPLC and ELISA experiments were carried out to evaluate the protein expression level and immunoreactivity of the purified CMV-IgM. A 910 kDa recombinant protein was successfully prepared and signal peptides (SigA-SigE) had an increased expressed CMV-IgM, which were 6.72, 5.19, 1.44, 1.85 and 1.98 times higher than that of the CMV 6# cell signal peptide SigF. In summary, this work provides a theoretical basis for the development of human-mouse chimeric CMV-IgM, and a novel route to increase the expression level of CMV-IgM.
Animals , Antibodies, Viral , Genetics , Allergy and Immunology , Cricetinae , Cytomegalovirus , Allergy and Immunology , Enzyme-Linked Immunosorbent Assay , Gene Expression , Humans , Immunoglobulin M , Allergy and Immunology , Mice , Protein Sorting Signals , Recombinant Fusion Proteins , Allergy and Immunology
Comparson of the immunogenicity of genotypeⅠJapanese encephalitis virus subunit vaccine candidate antigens / 生物工程学报
Ruiming YU; Zhancheng TIAN; Shandian GAO; Junzheng DU; Guangyuan LIU; Jianxun LUO; Hong YIN.
To screen the best genotypeⅠJapanese encephalitis virus subunit vaccine candidate antigens, the prMEIII gene, the polytope gene and the prMEIII-polytope fusion gene of the GenotypeⅠJapanese encephalitis virus GS strain were cloned into prokaryotic expression vector pET-30a. The recombinant proteins were obtained after the induction and purification. The prepared recombinant proteins were immunized to mice, and the immunogenicity of the subunit vaccine candidate antigens was evaluated through monitoring the humoral immune response by ELISA, detecting the neutralizing antibody titer by plaque reduction neutralization test, and testing the cell-mediated immune response by lymphocyte proliferation assay and cytokine profiling. The recombinant proteins with the molecular weights of 35 (prMEIII), 28 (polytope antigen) and 57 kDa (prMEIII-polytope) induced strong humoral and cellular immune responses in mice. Compared with prMEIII-polytope and polytope proteins, the prMEIII protein induced a significant expression of IL-2 and IFN-γ (P0.05). The study suggests that the prMEIII protein can be used for the development of the Japanese encephalitis virus subunit vaccine.
Animals , Antibodies, Viral , Blood , Antigens, Viral , Allergy and Immunology , Encephalitis Virus, Japanese , Allergy and Immunology , Encephalitis, Japanese , Allergy and Immunology , Immunogenicity, Vaccine , Mice , Mice, Inbred BALB C , Vaccines, Subunit , Allergy and Immunology , Viral Vaccines , Allergy and Immunology