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957 results on '"Qi, Jianxun"'

9. Deciphering a reliable synergistic bispecific strategy of rescuing antibodies for SARS-CoV-2 escape variants, including BA.2.86, EG.5.1, and JN.1

Author

Tong, Zhou, Tong, Jianyu, Lei, Wenwen, Xie, Yufeng, Cui, Yingzi, Jia, Guowen, Li, Shihua, Zhang, Zezhong, Cheng, Zhimin, Xing, Xiao, Ma, Haiyun, Deng, Lan, Zhang, Rong, Zhao, Xin, Liu, Kefang, Wang, Qihui, Qi, Jianxun, Huang, Haomin, Song, Rui, Su, Zhaoming, Wu, Guizhen, Lou, Jing, and Gao, George Fu

Published
2024
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13. Cryo-EM structure of severe fever with thrombocytopenia syndrome virus

Author

Du, Shouwen, Peng, Ruchao, Xu, Wang, Qu, Xiaoyun, Wang, Yuhang, Wang, Jiamin, Li, Letian, Tian, Mingyao, Guan, Yudong, Wang, Jigang, Wang, Guoqing, Li, Hao, Deng, Lingcong, Shi, Xiaoshuang, Ma, Yidan, Liu, Fengting, Sun, Minhua, Wei, Zhengkai, Jin, Ningyi, Liu, Wei, Qi, Jianxun, Liu, Quan, Liao, Ming, and Li, Chang

Published
2023
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14. Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants

Author

Zhao, Zhennan, Xie, Yufeng, Bai, Bin, Luo, Chunliang, Zhou, Jingya, Li, Weiwei, Meng, Yumin, Li, Linjie, Li, Dedong, Li, Xiaomei, Li, Xiaoxiong, Wang, Xiaoyun, Sun, Junqing, Xu, Zepeng, Sun, Yeping, Zhang, Wei, Fan, Zheng, Zhao, Xin, Wu, Linhuan, Ma, Juncai, Li, Odel Y., Shang, Guijun, Chai, Yan, Liu, Kefang, Wang, Peiyi, Gao, George F., and Qi, Jianxun

Published
2023
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31. Protective RBD-dimer vaccines against SARS-CoV-2 and its variants produced in glycoengineered Pichia pastoris.

Author

Zhao, Tongxin, Liu, Sheng, Wang, Pengyan, Zhang, Yanfang, Kang, Xinrui, Pan, Xiaoqian, Li, Linjie, Li, Dedong, Gao, Ping, An, Yaling, Song, Hao, Liu, Kefang, Qi, Jianxun, Zhao, Xin, Dai, Lianpan, Liu, Peipei, Wang, Peiyi, Wu, Guizhen, Zhu, Taicheng, and Xu, Kun

Subjects
SARS-CoV-2, PEPTIDE vaccines, COVID-19, PICHIA pastoris, COVID-19 vaccines
Abstract

Protective vaccines are crucial for preventing and controlling coronavirus disease 2019 (COVID-19). Updated vaccines are needed to confront the continuously evolving and circulating severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants. These vaccines should be safe, effective, amenable to easily scalable production, and affordable. Previously, we developed receptor binding domain (RBD) dimer-based protein subunit vaccines (ZF2001 and updated vaccines) in mammalian cells. In this study, we explored a strategy for producing RBD-dimer immunogens in Pichia pastoris. We found that wild-type P. pastoris produced hyperglycosylated RBD-dimer protein containing four N-glycosylation sites in P. pastoris. Therefore, we engineered the wild type P. pastoris (GS strain) into GSΔOCH1pAO by deleting the OCH1 gene (encoding α-1,6-mannosyltransferase enzyme) to decrease glycosylation, as well as by overexpressing the HIS4 gene (encoding histidine dehydrogenase) to increase histidine synthesis for better growth. In addition, RBD-dimer protein was truncated to remove the R328/F329 cleavage sites in P. pastoris. Several homogeneous RBD-dimer proteins were produced in the GSΔOCH1pAO strain, demonstrating the feasibility of using the P. pastoris expression system. We further resolved the cryo-EM structure of prototype-Beta RBD-dimer complexed with the neutralizing antibody CB6 to reveal the completely exposed immune epitopes of the RBDs. In a murine model, we demonstrated that the yeast-produced RBD-dimer induces robust and protective antibody responses, which is suitable for boosting immunization. This study developed the yeast system for producing SARS-CoV-2 RBD-dimer immunogens, providing a promising platform and pipeline for the future continuous updating and production of SARS-CoV-2 vaccines. Author summary: SARS-CoV-2 continuously circulates, resulting in infections and re-infections globally. COVID-19 vaccines can provide protection against disease and death caused by SARS-CoV-2. However, the immune responses induced by vaccination will wane gradually. In addition, new SARS-CoV-2 sub-variants emerge and show immune evasion. Therefore, inoculating with the updated COVID-19 vaccines is recommended for enhancing protection against the circulating SARS-CoV-2 sub-variants. Pichia pastoris is an eukaryotic system that enables fast and low-cost producing proteins with easy scale-up. In this study, we developed a strategy for producing SARS-CoV-2 RBD-dimer immunogens in glycoengineered Pichia pastoris with homogeneous glycosylation and high stability. The RBD antigen can be updated with the sequence of circulating sub-variants. In addition, mouse experiments demonstrated that the yeast-produced RBD-dimer vaccines induced robust and protective immune responses. This study provides a simple and promising approach to produce yeast-derived SARS-CoV-2 RBD-dimers as a boosting vaccine and guides the basis for the production of the other vaccines in Pichia pastoris. [ABSTRACT FROM AUTHOR]

Published
2024
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40. Research Progress on Harmful Characteristics and Mechanism of Walnut Late Frost.

Author

ZHANG Suilin, LI Yang, LI Yan, ZHANG Yunqi, QI Jianxun, and HOU Zhixia

Subjects
FROST, WALNUT, CATALASE, LOW temperatures, SUPEROXIDE dismutase, OSMOREGULATION, PEROXIDASE
Abstract

The occurrence of early spring and late frost damage brought severe challenges to the production of walnuts in China, seriously affecting their growth, development, yield and revenue. In order to clarify the harmful characteristics and influencing mechanisms of late frost on walnuts in China, the influencing factors of the degree of damage caused by late frost on walnuts, as well as the changes in physiological and biochemical indicators and molecular mechanisms in response to low temperature stress were reviewed. It was found that research on physiological changes focused on the three aspects including cell membrane system (relative conductivity), antioxidant system (malondialdehyde, superoxide dismutase, peroxidase and catalase) and osmoregulation substances (soluble sugars, soluble protein and proline), in addition, the expression levels of genes such as JrPAL, JrJAZ, JrGRAS, JrICE1, JrCBF/JrDREB1, JrCOR, JrWRKY, JrDHN, JrGST, and JrPUB were induced by low temperature stress. And prospects were put for future research directions, which provided scientific basis for further exploring the response mechanism of walnuts to late frost damage and adopting effective production measures. [ABSTRACT FROM AUTHOR]

Published
2024
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41. An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism.

Author

Song, Hao, Qi, Jianxun, Khedri, Zahra, Diaz, Sandra, Yu, Hai, Chen, Xi, Varki, Ajit, Shi, Yi, and Gao, George F

Subjects
Animals, Cattle, Swine, Dogs, Humans, Thogotovirus, Orthomyxoviridae Infections, Hemagglutinin Glycoproteins, Influenza Virus, Viral Fusion Proteins, Blotting, Western, Crystallography, X-Ray, Protein Array Analysis, Binding Sites, Protein Conformation, Virus Internalization, Madin Darby Canine Kidney Cells, Blotting, Western, Crystallography, X-Ray, Hemagglutinin Glycoproteins, Influenza Virus, Virology, Microbiology, Immunology, Medical Microbiology
Abstract

Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health.

Published
2016

42. Correction: An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism

Author

Song, Hao, Qi, Jianxun, Khedri, Zahra, Diaz, Sandra, Yu, Hai, Chen, Xi, Varki, Ajit, Shi, Yi, and Gao, George F

Subjects
Medical Microbiology, Biomedical and Clinical Sciences, Clinical Sciences, Biological Sciences, Emerging Infectious Diseases, Infectious Diseases, Biodefense, Influenza, Pneumonia & Influenza, Prevention, Vaccine Related, 2.2 Factors relating to the physical environment, Aetiology, Infection, Animals, Binding Sites, Blotting, Western, Cattle, Crystallography, X-Ray, Dogs, Hemagglutinin Glycoproteins, Influenza Virus, Humans, Madin Darby Canine Kidney Cells, Orthomyxoviridae Infections, Protein Array Analysis, Protein Conformation, Swine, Thogotovirus, Viral Fusion Proteins, Virus Internalization, Microbiology, Immunology, Virology, Medical microbiology
Abstract

Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health.

Published
2016

46. The molecular basis for SARS-CoV-2 binding to dog ACE2

Author

Zhang, Zengyuan, Zhang, Yanfang, Liu, Kefang, Li, Yan, Lu, Qiong, Wang, Qingling, Zhang, Yuqin, Wang, Liang, Liao, Hanyi, Zheng, Anqi, Ma, Sufang, Fan, Zheng, Li, Huifang, Huang, Weijin, Bi, Yuhai, Zhao, Xin, Wang, Qihui, Gao, George F., Xiao, Haixia, Tong, Zhou, Qi, Jianxun, and Sun, Yeping

Published
2021
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