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Start Over Author "Zhang, Baoshan" Publisher american society for microbiology
18 results on '"Zhang, Baoshan"'

1. Diverse Murine Vaccinations Reveal Distinct Antibody Classes to Target Fusion Peptide and Variation in Peptide Length to Improve HIV Neutralization

Author

Sastry, Mallika, primary, Changela, Anita, additional, Gorman, Jason, additional, Xu, Kai, additional, Chuang, Gwo-Yu, additional, Shen, Chen-Hsiang, additional, Cheng, Cheng, additional, Geng, Hui, additional, O'Dell, Sijy, additional, Ou, Li, additional, Rawi, Reda, additional, Reveiz, Mateo, additional, Stewart-Jones, Guillaume B. E., additional, Wang, Shuishu, additional, Zhang, Baoshan, additional, Zhou, Tongqing, additional, Biju, Andrea, additional, Chambers, Michael, additional, Chen, Xuejun, additional, Corrigan, Angela R., additional, Lin, Bob C., additional, Louder, Mark K., additional, McKee, Krisha, additional, Nazzari, Alexandra F., additional, Olia, Adam S., additional, Parchment, Danealle K., additional, Sarfo, Edward K., additional, Stephens, Tyler, additional, Stuckey, Jonathan, additional, Tsybovsky, Yaroslav, additional, Verardi, Raffaello, additional, Wang, Yiran, additional, Zheng, Cheng-Yan, additional, Chen, Yuling, additional, Doria-Rose, Nicole A., additional, McDermott, Adrian B., additional, Mascola, John R., additional, and Kwong, Peter D., additional

Published
2023
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2. Development of a 3Mut-Apex-Stabilized Envelope Trimer That Expands HIV-1 Neutralization Breadth When Used To Boost Fusion Peptide-Directed Vaccine-Elicited Responses

Author

Chuang, Gwo-Yu, primary, Lai, Yen-Ting, additional, Boyington, Jeffrey C., additional, Cheng, Cheng, additional, Geng, Hui, additional, Narpala, Sandeep, additional, Rawi, Reda, additional, Schmidt, Stephen D., additional, Tsybovsky, Yaroslav, additional, Verardi, Raffaello, additional, Xu, Kai, additional, Yang, Yongping, additional, Zhang, Baoshan, additional, Chambers, Michael, additional, Changela, Anita, additional, Corrigan, Angela R., additional, Kong, Rui, additional, Olia, Adam S., additional, Ou, Li, additional, Sarfo, Edward K., additional, Wang, Shuishu, additional, Wu, Winston, additional, Doria-Rose, Nicole A., additional, McDermott, Adrian B., additional, Mascola, John R., additional, and Kwong, Peter D., additional

Published
2020
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3. Residues 28 to 39 of the Extracellular Loop 1 of Chicken Na + /H + Exchanger Type I Mediate Cell Binding and Entry of Subgroup J Avian Leukosis Virus

Author

Guan, Xiaolu, primary, Zhang, Yao, additional, Yu, Mengmeng, additional, Ren, Chaoqi, additional, Gao, Yanni, additional, Yun, Bingling, additional, Liu, Yongzhen, additional, Wang, Yongqiang, additional, Qi, Xiaole, additional, Liu, Changjun, additional, Cui, Hongyu, additional, Zhang, Yanping, additional, Gao, Li, additional, Li, Kai, additional, Pan, Qing, additional, Zhang, Baoshan, additional, Wang, Xiaomei, additional, and Gao, Yulong, additional

Published
2018
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4. Optimization of the Solubility of HIV-1-Neutralizing Antibody 10E8 through Somatic Variation and Structure-Based Design

Author

Kwon, Young D., primary, Georgiev, Ivelin S., additional, Ofek, Gilad, additional, Zhang, Baoshan, additional, Asokan, Mangaiarkarasi, additional, Bailer, Robert T., additional, Bao, Amy, additional, Caruso, William, additional, Chen, Xuejun, additional, Choe, Misook, additional, Druz, Aliaksandr, additional, Ko, Sung-Youl, additional, Louder, Mark K., additional, McKee, Krisha, additional, O'Dell, Sijy, additional, Pegu, Amarendra, additional, Rudicell, Rebecca S., additional, Shi, Wei, additional, Wang, Keyun, additional, Yang, Yongping, additional, Alger, Mandy, additional, Bender, Michael F., additional, Carlton, Kevin, additional, Cooper, Jonathan W., additional, Blinn, Julie, additional, Eudailey, Joshua, additional, Lloyd, Krissey, additional, Parks, Robert, additional, Alam, S. Munir, additional, Haynes, Barton F., additional, Padte, Neal N., additional, Yu, Jian, additional, Ho, David D., additional, Huang, Jinghe, additional, Connors, Mark, additional, Schwartz, Richard M., additional, Mascola, John R., additional, and Kwong, Peter D., additional

Published
2016
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5. Single-Chain Soluble BG505.SOSIP gp140 Trimers as Structural and Antigenic Mimics of Mature Closed HIV-1 Env

Author

Georgiev, Ivelin S., primary, Joyce, M. Gordon, additional, Yang, Yongping, additional, Sastry, Mallika, additional, Zhang, Baoshan, additional, Baxa, Ulrich, additional, Chen, Rita E., additional, Druz, Aliaksandr, additional, Lees, Christopher R., additional, Narpala, Sandeep, additional, Schön, Arne, additional, Van Galen, Joseph, additional, Chuang, Gwo-Yu, additional, Gorman, Jason, additional, Harned, Adam, additional, Pancera, Marie, additional, Stewart-Jones, Guillaume B. E., additional, Cheng, Cheng, additional, Freire, Ernesto, additional, McDermott, Adrian B., additional, Mascola, John R., additional, and Kwong, Peter D., additional

Published
2015
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6. Neutralization Properties of Simian Immunodeficiency Viruses Infecting Chimpanzees and Gorillas

Author

Barbian, Hannah J., primary, Decker, Julie M., additional, Bibollet-Ruche, Frederic, additional, Galimidi, Rachel P., additional, West, Anthony P., additional, Learn, Gerald H., additional, Parrish, Nicholas F., additional, Iyer, Shilpa S., additional, Li, Yingying, additional, Pace, Craig S., additional, Song, Ruijiang, additional, Huang, Yaoxing, additional, Denny, Thomas N., additional, Mouquet, Hugo, additional, Martin, Loic, additional, Acharya, Priyamvada, additional, Zhang, Baoshan, additional, Kwong, Peter D., additional, Mascola, John R., additional, Verrips, C. Theo, additional, Strokappe, Nika M., additional, Rutten, Lucy, additional, McCoy, Laura E., additional, Weiss, Robin A., additional, Brown, Corrine S., additional, Jackson, Raven, additional, Silvestri, Guido, additional, Connors, Mark, additional, Burton, Dennis R., additional, Shaw, George M., additional, Nussenzweig, Michel C., additional, Bjorkman, Pamela J., additional, Ho, David D., additional, Farzan, Michael, additional, and Hahn, Beatrice H., additional

Published
2015
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7. Structural Definition of an Antibody-Dependent Cellular Cytotoxicity Response Implicated in Reduced Risk for HIV-1 Infection

Author

Acharya, Priyamvada, primary, Tolbert, William D., additional, Gohain, Neelakshi, additional, Wu, Xueji, additional, Yu, Lei, additional, Liu, Tongyun, additional, Huang, Wensheng, additional, Huang, Chih-chin, additional, Kwon, Young Do, additional, Louder, Robert K., additional, Luongo, Timothy S., additional, McLellan, Jason S., additional, Pancera, Marie, additional, Yang, Yongping, additional, Zhang, Baoshan, additional, Flinko, Robin, additional, Foulke, James S., additional, Sajadi, Mohammad M., additional, Kamin-Lewis, Roberta, additional, Robinson, James E., additional, Martin, Loïc, additional, Kwong, Peter D., additional, Guan, Yongjun, additional, DeVico, Anthony L., additional, Lewis, George K., additional, and Pazgier, Marzena, additional

Published
2014
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8. Structural Basis for HIV-1 Neutralization by 2F5-Like Antibodies m66 and m66.6

Author

Ofek, Gilad, primary, Zirkle, Brett, additional, Yang, Yongping, additional, Zhu, Zhongyu, additional, McKee, Krisha, additional, Zhang, Baoshan, additional, Chuang, Gwo-Yu, additional, Georgiev, Ivelin S., additional, O'Dell, Sijy, additional, Doria-Rose, Nicole, additional, Mascola, John R., additional, Dimitrov, Dimiter S., additional, and Kwong, Peter D., additional

Published
2014
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9. Outer Domain of HIV-1 gp120: Antigenic Optimization, Structural Malleability, and Crystal Structure with Antibody VRC-PG04

Author

Joyce, M. Gordon, primary, Kanekiyo, Masaru, additional, Xu, Ling, additional, Biertümpfel, Christian, additional, Boyington, Jeffrey C., additional, Moquin, Stephanie, additional, Shi, Wei, additional, Wu, Xueling, additional, Yang, Yongping, additional, Yang, Zhi-Yong, additional, Zhang, Baoshan, additional, Zheng, Anqi, additional, Zhou, Tongqing, additional, Zhu, Jiang, additional, Mascola, John R., additional, Kwong, Peter D., additional, and Nabel, Gary J., additional

Published
2013
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10. Analysis of a Clonal Lineage of HIV-1 Envelope V2/V3 Conformational Epitope-Specific Broadly Neutralizing Antibodies and Their Inferred Unmutated Common Ancestors

Author

Bonsignori, Mattia, primary, Hwang, Kwan-Ki, additional, Chen, Xi, additional, Tsao, Chun-Yen, additional, Morris, Lynn, additional, Gray, Elin, additional, Marshall, Dawn J., additional, Crump, John A., additional, Kapiga, Saidi H., additional, Sam, Noel E., additional, Sinangil, Faruk, additional, Pancera, Marie, additional, Yongping, Yang, additional, Zhang, Baoshan, additional, Zhu, Jiang, additional, Kwong, Peter D., additional, O'Dell, Sijy, additional, Mascola, John R., additional, Wu, Lan, additional, Nabel, Gary J., additional, Phogat, Sanjay, additional, Seaman, Michael S., additional, Whitesides, John F., additional, Moody, M. Anthony, additional, Kelsoe, Garnett, additional, Yang, Xinzhen, additional, Sodroski, Joseph, additional, Shaw, George M., additional, Montefiori, David C., additional, Kepler, Thomas B., additional, Tomaras, Georgia D., additional, Alam, S. Munir, additional, Liao, Hua-Xin, additional, and Haynes, Barton F., additional

Published
2011
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11. Immunotypes of a Quaternary Site of HIV-1 Vulnerability and Their Recognition by Antibodies

Author

Wu, Xueling, primary, Changela, Anita, additional, O'Dell, Sijy, additional, Schmidt, Stephen D., additional, Pancera, Marie, additional, Yang, Yongping, additional, Zhang, Baoshan, additional, Gorny, Miroslaw K., additional, Phogat, Sanjay, additional, Robinson, James E., additional, Stamatatos, Leonidas, additional, Zolla-Pazner, Susan, additional, Kwong, Peter D., additional, and Mascola, John R., additional

Published
2011
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12. Crystal Structure of Human Antibody 2909 Reveals Conserved Features of Quaternary Structure-Specific Antibodies That Potently Neutralize HIV-1

Author

Changela, Anita, primary, Wu, Xueling, additional, Yang, Yongping, additional, Zhang, Baoshan, additional, Zhu, Jiang, additional, Nardone, Glenn A., additional, O'Dell, Sijy, additional, Pancera, Marie, additional, Gorny, Miroslaw K., additional, Phogat, Sanjay, additional, Robinson, James E., additional, Stamatatos, Leonidas, additional, Zolla-Pazner, Susan, additional, Mascola, John R., additional, and Kwong, Peter D., additional

Published
2011
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17. Residues 28 to 39 of the Extracellular Loop 1 of Chicken Na + /H + Exchanger Type I Mediate Cell Binding and Entry of Subgroup J Avian Leukosis Virus.

Author

Guan X, Zhang Y, Yu M, Ren C, Gao Y, Yun B, Liu Y, Wang Y, Qi X, Liu C, Cui H, Zhang Y, Gao L, Li K, Pan Q, Zhang B, Wang X, and Gao Y

Subjects
Amino Acids metabolism, Animals, Avian Leukosis virology, Avian Leukosis Virus chemistry, Avian Leukosis Virus genetics, Chickens, Humans, Point Mutation, Receptors, Virus genetics, Sodium-Hydrogen Exchangers genetics, Amino Acids chemistry, Avian Leukosis Virus metabolism, Receptors, Virus metabolism, Sodium-Hydrogen Exchangers chemistry, Sodium-Hydrogen Exchangers metabolism, Virus Attachment, Virus Internalization
Abstract

Chicken Na + /H + exchanger type I (chNHE1), a multispan transmembrane protein, is a cellular receptor of the subgroup J avian leukosis virus (ALV-J). To identify the functional determinants of chNHE1 responsible for the ALV-J receptor activity, a series of chimeric receptors was created by exchanging the extracellular loops (ECL) of human NHE1 (huNHE1) and chNHE1 and by ECL replacement with a hemagglutinin (HA) tag. These chimeric receptors then were used in binding and entry assays to map the minimal ALV-J gp85-binding domain of chNHE1. We show that ECL1 of chNHE1 (chECL1) is the critical functional ECL that interacts directly with ALV-J gp85; ECL3 is also involved in ALV-J gp85 binding. Amino acid residues 28 to 39 of the N-terminal membrane-proximal region of chECL1 constitute the minimal domain required for chNHE1 binding of ALV-J gp85. These residues are sufficient to mediate viral entry into ALV-J nonpermissive cells. Point mutation analysis revealed that A30, V33, W38, and E39 of chECL1 are the key residues mediating the binding between chNHE1 and ALV-J gp85. Further, the replacement of residues 28 to 39 of huNHE1 with the corresponding chNHE1 residues converted the nonfunctional ALV-J receptor huNHE1 to a functional one. Importantly, soluble chECL1 and huECL1 harboring chNHE1 residues 28 to 39 both could effectively block ALV-J infection. Collectively, our findings indicate that residues 28 to 39 of chNHE1 constitute a domain that is critical for receptor function and mediate ALV-J entry. IMPORTANCE chNHE1 is a cellular receptor of ALV-J, a retrovirus that causes infections in chickens and serious economic losses in the poultry industry. Until now, the domains determining the chNHE1 receptor function remained unknown. We demonstrate that chECL1 is critical for receptor function, with residues 28 to 39 constituting the minimal functional domain responsible for chNHE1 binding of ALV-J gp85 and efficiently mediating ALV-J cell entry. These residues are located in the membrane-proximal region of the N terminus of chECL1, suggesting that the binding site of ALV-J gp85 on chNHE1 is probably located on the apex of the molecule; the receptor-binding mode might be different from that of retroviruses. We also found that soluble chECL1, as well as huECL1 harboring chNHE1 residues 28 to 39, effectively blocked ALV-J infection. These findings contribute to a better understanding of the ALV-J infection mechanism and also provide new insights into the control strategies for ALV-J infection., (Copyright © 2017 American Society for Microbiology.)

Published
2017
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18. Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo.

Author

Rudicell RS, Kwon YD, Ko SY, Pegu A, Louder MK, Georgiev IS, Wu X, Zhu J, Boyington JC, Chen X, Shi W, Yang ZY, Doria-Rose NA, McKee K, O'Dell S, Schmidt SD, Chuang GY, Druz A, Soto C, Yang Y, Zhang B, Zhou T, Todd JP, Lloyd KE, Eudailey J, Roberts KE, Donald BR, Bailer RT, Ledgerwood J, Mullikin JC, Shapiro L, Koup RA, Graham BS, Nason MC, Connors M, Haynes BF, Rao SS, Roederer M, Kwong PD, Mascola JR, and Nabel GJ

Subjects
Animals, Antibodies, Neutralizing administration & dosage, Antibodies, Neutralizing genetics, HIV Antibodies administration & dosage, HIV Antibodies genetics, HIV-1 genetics, Macaca mulatta, Male, Molecular Sequence Data, Sequence Analysis, DNA, Antibodies, Neutralizing immunology, HIV Antibodies immunology, HIV-1 immunology, Immunization, Passive methods, Simian Acquired Immunodeficiency Syndrome prevention & control
Abstract

Unlabelled: Over the past 5 years, a new generation of highly potent and broadly neutralizing HIV-1 antibodies has been identified. These antibodies can protect against lentiviral infection in nonhuman primates (NHPs), suggesting that passive antibody transfer would prevent HIV-1 transmission in humans. To increase the protective efficacy of such monoclonal antibodies, we employed next-generation sequencing, computational bioinformatics, and structure-guided design to enhance the neutralization potency and breadth of VRC01, an antibody that targets the CD4 binding site of the HIV-1 envelope. One variant, VRC07-523, was 5- to 8-fold more potent than VRC01, neutralized 96% of viruses tested, and displayed minimal autoreactivity. To compare its protective efficacy to that of VRC01 in vivo, we performed a series of simian-human immunodeficiency virus (SHIV) challenge experiments in nonhuman primates and calculated the doses of VRC07-523 and VRC01 that provide 50% protection (EC50). VRC07-523 prevented infection in NHPs at a 5-fold lower concentration than VRC01. These results suggest that increased neutralization potency in vitro correlates with improved protection against infection in vivo, documenting the improved functional efficacy of VRC07-523 and its potential clinical relevance for protecting against HIV-1 infection in humans., Importance: In the absence of an effective HIV-1 vaccine, alternative strategies are needed to block HIV-1 transmission. Direct administration of HIV-1-neutralizing antibodies may be able to prevent HIV-1 infections in humans. This approach could be especially useful in individuals at high risk for contracting HIV-1 and could be used together with antiretroviral drugs to prevent infection. To optimize the chance of success, such antibodies can be modified to improve their potency, breadth, and in vivo half-life. Here, knowledge of the structure of a potent neutralizing antibody, VRC01, that targets the CD4-binding site of the HIV-1 envelope protein was used to engineer a next-generation antibody with 5- to 8-fold increased potency in vitro. When administered to nonhuman primates, this antibody conferred protection at a 5-fold lower concentration than the original antibody. Our studies demonstrate an important correlation between in vitro assays used to evaluate the therapeutic potential of antibodies and their in vivo effectiveness., (Copyright © 2014, American Society for Microbiology. All Rights Reserved.)

Published
2014
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