25 results on '"Wang, Haoqing"'
Search Results
2. Neuroanatomical and clinical factors predicting future cognitive impairment
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Imms, Phoebe, Chaudhari, Nikhil N., Chowdhury, Nahian F., Wang, Haoqing, Yu, Xiaokun, Amgalan, Anar, and Irimia, Andrei
- Abstract
Identifying cognitively normal (CN) older adults who will convert to cognitive impairment (CI) due to Alzheimer’s disease is crucial for early intervention. Clinical and neuroimaging measures were acquired from 301 CN adults who converted to CI within 15 years of baseline, and 294 who did not. Regional volumes and brain age measures were extracted from T1-weighted magnetic resonance images. Linear discriminant analysis compared non-converters’ characteristics against those of short-, mid-, and long-term converters. Conversion was associated with clinical measures such as hearing impairment and self-reported memory decline. Converters’ brain volumes were smaller than non-converters’ across 48 frontal, temporal, and subcortical structures. Brain age measures of 12 structures were correlated with shorter times to conversion. Conversion prediction accuracy increased from 81.5% to 90.5% as time to conversion decreased. Proximity to CI conversion is foreshadowed by anatomic features of brain aging that enhance the accuracy of predicting conversion.
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- 2024
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3. Stepwise activation of a metabotropic glutamate receptor
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Krishna Kumar, Kaavya, Wang, Haoqing, Habrian, Chris, Latorraca, Naomi R., Xu, Jun, O’Brien, Evan S., Zhang, Chensong, Montabana, Elizabeth, Koehl, Antoine, Marqusee, Susan, Isacoff, Ehud Y., and Kobilka, Brian K.
- Abstract
Metabotropic glutamate receptors belong to a family of G protein-coupled receptors that are obligate dimers and possess a large extracellular ligand-binding domain that is linked via a cysteine-rich domain to their 7-transmembrane domain1. Upon activation, these receptors undergo a large conformational change to transmit the ligand binding signal from the extracellular ligand-binding domain to the G protein-coupling 7-transmembrane domain2. In this manuscript, we propose a model for a sequential, multistep activation mechanism of metabotropic glutamate receptor subtype 5. We present a series of structures in lipid nanodiscs, from inactive to fully active, including agonist-bound intermediate states. Further, using bulk and single-molecule fluorescence imaging, we reveal distinct receptor conformations upon allosteric modulator and G protein binding.
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- 2024
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4. A µ-opioid receptor modulator that works cooperatively with naloxone
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O’Brien, Evan S., Rangari, Vipin Ashok, El Daibani, Amal, Eans, Shainnel O., Hammond, Haylee R., White, Elizabeth, Wang, Haoqing, Shiimura, Yuki, Krishna Kumar, Kaavya, Jiang, Qianru, Appourchaux, Kevin, Huang, Weijiao, Zhang, Chensong, Kennedy, Brandon J., Mathiesen, Jesper M., Che, Tao, McLaughlin, Jay P., Majumdar, Susruta, and Kobilka, Brian K.
- Abstract
The µ-opioid receptor (µOR) is a well-established target for analgesia1, yet conventional opioid receptor agonists cause serious adverse effects, notably addiction and respiratory depression. These factors have contributed to the current opioid overdose epidemic driven by fentanyl2, a highly potent synthetic opioid. µOR negative allosteric modulators (NAMs) may serve as useful tools in preventing opioid overdose deaths, but promising chemical scaffolds remain elusive. Here we screened a large DNA-encoded chemical library against inactive µOR, counter-screening with active, G-protein and agonist-bound receptor to ‘steer’ hits towards conformationally selective modulators. We discovered a NAM compound with high and selective enrichment to inactive µOR that enhances the affinity of the key opioid overdose reversal molecule, naloxone. The NAM works cooperatively with naloxone to potently block opioid agonist signalling. Using cryogenic electron microscopy, we demonstrate that the NAM accomplishes this effect by binding a site on the extracellular vestibule in direct contact with naloxone while stabilizing a distinct inactive conformation of the extracellular portions of the second and seventh transmembrane helices. The NAM alters orthosteric ligand kinetics in therapeutically desirable ways and works cooperatively with low doses of naloxone to effectively inhibit various morphine-induced and fentanyl-induced behavioural effects in vivo while minimizing withdrawal behaviours. Our results provide detailed structural insights into the mechanism of negative allosteric modulation of the µOR and demonstrate how this can be exploited in vivo.
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- 2024
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5. Design of magnesium-based solid-state hydrogen storage materials for automobile battery application
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Fu, Yabo, Prakash, Kolla Bhanu, and Wang, Haoqing
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- 2023
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6. Mechano-covalent protection of coagulation factor VIII by von Willebrand factor
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Butera, Diego, Wang, Haoqing Jerry, Woon, Heng-Giap, Zhao, Yunduo Charles, Ju, Lining Arnold, and Hogg, Philip J.
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•Bleeding arrest is critically dependent on FVIII binding to VWF in the shear forces of the circulation.•FVIII binding involves dynamic changes in the covalent states of several VWF disulfides that is required for a productive interaction.
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- 2023
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7. Structure-based design of bitopic ligands for the µ-opioid receptor
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Faouzi, Abdelfattah, Wang, Haoqing, Zaidi, Saheem A., DiBerto, Jeffrey F., Che, Tao, Qu, Qianhui, Robertson, Michael J., Madasu, Manish K., El Daibani, Amal, Varga, Balazs R., Zhang, Tiffany, Ruiz, Claudia, Liu, Shan, Xu, Jin, Appourchaux, Kevin, Slocum, Samuel T., Eans, Shainnel O., Cameron, Michael D., Al-Hasani, Ream, Pan, Ying Xian, Roth, Bryan L., McLaughlin, Jay P., Skiniotis, Georgios, Katritch, Vsevolod, Kobilka, Brian K., and Majumdar, Susruta
- Abstract
Mu-opioid receptor (µOR) agonists such as fentanyl have long been used for pain management, but are considered a major public health concern owing to their adverse side effects, including lethal overdose1. Here, in an effort to design safer therapeutic agents, we report an approach targeting a conserved sodium ion-binding site2found in µOR3and many other class A G-protein-coupled receptors with bitopic fentanyl derivatives that are functionalized via a linker with a positively charged guanidino group. Cryo-electron microscopy structures of the most potent bitopic ligands in complex with µOR highlight the key interactions between the guanidine of the ligands and the key Asp2.50residue in the Na+site. Two bitopics (C5 and C6 guano) maintain nanomolar potency and high efficacy at Gisubtypes and show strongly reduced arrestin recruitment—one (C6 guano) also shows the lowest Gzefficacy among the panel of µOR agonists, including partial and biased morphinan and fentanyl analogues. In mice, C6 guano displayed µOR-dependent antinociception with attenuated adverse effects, supporting the µOR sodium ion-binding site as a potential target for the design of safer analgesics. In general, our study suggests that bitopic ligands that engage the sodium ion-binding pocket in class A G-protein-coupled receptors can be designed to control their efficacy and functional selectivity profiles for Gi, Goand Gzsubtypes and arrestins, thus modulating their in vivo pharmacology.
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- 2023
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8. Discovery of VH domains that allosterically inhibit ENPP1
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Solomon, Paige E., Bracken, Colton J., Carozza, Jacqueline A., Wang, Haoqing, Young, Elizabeth P., Wellner, Alon, Liu, Chang C., Sweet-Cordero, E. Alejandro, Li, Lingyin, and Wells, James A.
- Abstract
Ectodomain phosphatase/phosphodiesterase-1 (ENPP1) is overexpressed on cancer cells and functions as an innate immune checkpoint by hydrolyzing extracellular cyclic guanosine monophosphate adenosine monophosphate (cGAMP). Biologic inhibitors have not yet been reported and could have substantial therapeutic advantages over current small molecules because they can be recombinantly engineered into multifunctional formats and immunotherapies. Here we used phage and yeast display coupled with in cellulo evolution to generate variable heavy (VH) single-domain antibodies against ENPP1 and discovered a VH domain that allosterically inhibited the hydrolysis of cGAMP and adenosine triphosphate (ATP). We solved a 3.2 Å-resolution cryo-electron microscopy structure for the VH inhibitor complexed with ENPP1 that confirmed its new allosteric binding pose. Finally, we engineered the VH domain into multispecific formats and immunotherapies, including a bispecific fusion with an anti-PD-L1 checkpoint inhibitor that showed potent cellular activity.
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- 2023
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9. SimH: A Novel Representation Learning Model With Activation and Projection Mechanisms for COVID-19 Knowledge Bases
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Su, Qing, Ou, Enhai, Sun, Yuping, Lv, Chunyan, Xie, Guobo, Wang, Haoqing, and Huang, Honglin
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The emergence of coronavirus disease 2019 (COVID-19) has had a significant impact on healthcare and the economy. With representation learning applied in constructing COVID-19 knowledge graphs, abundant COVID-19-related knowledge collected by clinicians and scientists all over the world can be utilized to deepen their understanding of the mechanism and related biological functions of the disease. However, most existing representation learning models cannot deal well with COVID-19 knowledge graph due to its low-connected star-like structure and various complex nonlinear relationships. Besides, lacking reliable negative triplets is also a difficult problem, yet to be adequately resolved. In this article, we propose a novel representation learning model called translation on hyperplanes with an activation operation and similar semantic sampling (SimH) for COVID-19 knowledge graphs. In our proposed SimH, an activation operation is designed to provide additional interaction features for low-in-degree entities. Then the hyperplane projection technique is introduced to the distance-based scoring function so that those complex nonlinear relationships can be modeled with lower complexity maintained in comparison with other nonlinear models. Moreover, a negative triplet sampling method that adaptively replaces entities with similar semantics is introduced to generate reliable negative triplets. To verify the effectiveness of SimH, extensive experiments are conducted on the COVID-19-Concepts dataset. The experimental results show that our SimH model achieves significant improvements in prediction and classification accuracy over existing knowledge representation learning models.
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- 2022
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10. Insights into distinct signaling profiles of the µOR activated by diverse agonists
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Qu, Qianhui, Huang, Weijiao, Aydin, Deniz, Paggi, Joseph M., Seven, Alpay B., Wang, Haoqing, Chakraborty, Soumen, Che, Tao, DiBerto, Jeffrey F., Robertson, Michael J., Inoue, Asuka, Suomivuori, Carl-Mikael, Roth, Bryan L., Majumdar, Susruta, Dror, Ron O., Kobilka, Brian K., and Skiniotis, Georgios
- Abstract
Drugs targeting the μ-opioid receptor (μOR) are the most effective analgesics available but are also associated with fatal respiratory depression through a pathway that remains unclear. Here we investigated the mechanistic basis of action of lofentanil (LFT) and mitragynine pseudoindoxyl (MP), two μOR agonists with different safety profiles. LFT, one of the most lethal opioids, and MP, a kratom plant derivative with reduced respiratory depression in animal studies, exhibited markedly different efficacy profiles for G protein subtype activation and β-arrestin recruitment. Cryo-EM structures of μOR-Gi1 complex with MP (2.5 Å) and LFT (3.2 Å) revealed that the two ligands engage distinct subpockets, and molecular dynamics simulations showed additional differences in the binding site that promote distinct active-state conformations on the intracellular side of the receptor where G proteins and β-arrestins bind. These observations highlight how drugs engaging different parts of the μOR orthosteric pocket can lead to distinct signaling outcomes.
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- 2022
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11. Maltose-bis(hydroxymethyl)phenol (MBPs) and Maltose-tris(hydroxymethyl)phenol (MTPs) Amphiphiles for Membrane Protein Stability
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Ehsan, Muhammad, Wang, Haoqing, Cecchetti, Cristina, Mortensen, Jonas S., Du, Yang, Hariharan, Parameswaran, Nygaard, Andreas, Lee, Ho Jin, Ghani, Lubna, Guan, Lan, Loland, Claus J., Byrne, Bernadette, Kobilka, Brian K., and Chae, Pil Seok
- Abstract
Membrane protein structures provide a fundamental understanding of their molecular actions and are of importance for drug development. Detergents are widely used to solubilize, stabilize, and crystallize membrane proteins, but membrane proteins solubilized in conventional detergents are prone to denaturation and aggregation. Thus, developing novel detergents with enhanced efficacy for protein stabilization remains important. We report herein the design and synthesis of a class of phenol-derived maltoside detergents. Using two different linkers, we prepared two sets of new detergents, designated maltose-bis(hydroxymethyl)phenol (MBPs) and maltose-tris(hydroxymethyl)phenol (MTPs). The evaluation of these detergents with three transporters and two G-protein coupled receptors allowed us to identify a couple of new detergents (MBP-C9 and MTP-C12) that consistently conferred enhanced stability to all tested proteins compared to a gold standard detergent (DDM). Furthermore, the data analysis based on the detergent structures provides key detergent features responsible for membrane protein stabilization that together will facilitate the future design of novel detergents.
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- 2021
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12. Negative allosteric modulation of the µ-opioid receptor
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O'Brien, Evan S., Rangari, Vipin A., El Daibani, Amal, Eans, Shainnel O., White, Betsy, Wang, Haoqing, Shiimura, Yuki, Kumar, Kaavya Krishna, Appourchaux, Kevin, Zhang, Chensong, Mathiesen, Jesper M., Che, Tao, McLaughlin, Jay P., Majumdar, Susruta, and Kobilka, Brian K.
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- 2024
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13. Signaling Modulation Mediated by Ligand Water Interactions with the Sodium Site at μOR
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Ople, Rohini S., Ramos-Gonzalez, Nokomis, Li, Qiongyu, Sobecks, Briana L., Aydin, Deniz, Powers, Alexander S., Faouzi, Abdelfattah, Polacco, Benjamin J., Bernhard, Sarah M., Appourchaux, Kevin, Sribhashyam, Sashrik, Eans, Shainnel O., Tsai, Bowen A., Dror, Ron O., Varga, Balazs R., Wang, Haoqing, Hüttenhain, Ruth, McLaughlin, Jay P., and Majumdar, Susruta
- Abstract
The mu opioid receptor (μOR) is a target for clinically used analgesics. However, adverse effects, such as respiratory depression and physical dependence, necessitate the development of alternative treatments. Recently we reported a novel strategy to design functionally selective opioids by targeting the sodium binding allosteric site in μOR with a supraspinally active analgesic named C6guano. Presently, to improve systemic activity of this ligand, we used structure-based design, identifying a new ligand named RO76where the flexible alkyl linker and polar guanidine guano group is swapped with a benzyl alcohol, and the sodium site is targeted indirectly through waters. A cryoEM structure of RO76bound to the μOR-Gicomplex confirmed that RO76interacts with the sodium site residues through a water molecule, unlike C6guanowhich engages the sodium site directly. Signaling assays coupled with APEX based proximity labeling show binding in the sodium pocket modulates receptor efficacy and trafficking. In mice, RO76was systemically active in tail withdrawal assays and showed reduced liabilities compared to those of morphine. In summary, we show that targeting water molecules in the sodium binding pocket may be an avenue to modulate signaling properties of opioids, and which may potentially be extended to other G-protein coupled receptors where this site is conserved.
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- 2024
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14. Author Correction: Stepwise activation of a metabotropic glutamate receptor
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Krishna Kumar, Kaavya, Wang, Haoqing, Habrian, Chris, Latorraca, Naomi R., Xu, Jun, O’Brien, Evan S., Zhang, Chensong, Montabana, Elizabeth, Koehl, Antoine, Marqusee, Susan, Isacoff, Ehud Y., and Kobilka, Brian K.
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- 2024
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15. Diastereomeric Cyclopentane-Based Maltosides (CPMs) as Tools for Membrane Protein Study
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Das, Manabendra, Mahler, Florian, Hariharan, Parameswaran, Wang, Haoqing, Du, Yang, Mortensen, Jonas S., Patallo, Eugenio Pérez, Ghani, Lubna, Glück, David, Lee, Ho Jin, Byrne, Bernadette, Loland, Claus J., Guan, Lan, Kobilka, Brian K., Keller, Sandro, and Chae, Pil Seok
- Abstract
Amphiphilic agents, called detergents, are invaluable tools for studying membrane proteins. However, membrane proteins encapsulated by conventional head-to-tail detergents tend to denature or aggregate, necessitating the development of structurally distinct molecules with improved efficacy. Here, a novel class of diastereomeric detergents with a cyclopentane core unit, designated cyclopentane-based maltosides (CPMs), were prepared and evaluated for their ability to solubilize and stabilize several model membrane proteins. A couple of CPMs displayed enhanced behavior compared with the benchmark conventional detergent, n-dodecyl-β-d-maltoside (DDM), for all the tested membrane proteins including two G-protein-coupled receptors (GPCRs). Furthermore, CPM-C12 was notable for its ability to confer enhanced membrane protein stability compared with the previously developed conformationally rigid NBMs [J. Am. Chem. Soc.2017, 139, 3072] and LMNG. The effect of the individual CPMs on protein stability varied depending on both the detergent configuration (cis/trans) and alkyl chain length, allowing us draw conclusions on the detergent structure–property–efficacy relationship. Thus, this study not only provides novel detergent tools useful for membrane protein research but also reports on structural features of the detergents critical for detergent efficacy in stabilizing membrane proteins.
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- 2020
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16. New Malonate-Derived Tetraglucoside Detergents for Membrane Protein Stability
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Ehsan, Muhammad, Katsube, Satoshi, Cecchetti, Cristina, Du, Yang, Mortensen, Jonas S., Wang, Haoqing, Nygaard, Andreas, Ghani, Lubna, Loland, Claus J., Kobilka, Brian K., Byrne, Bernadette, Guan, Lan, and Chae, Pil Seok
- Abstract
Membrane proteins are widely studied in detergent micelles, a membrane-mimetic system formed by amphiphilic compounds. However, classical detergents have serious limitations in their utility, particularly for unstable proteins such as eukaryotic membrane proteins and membrane protein complexes, and thus, there is an unmet need for novel amphiphiles with enhanced ability to stabilize membrane proteins. Here, we developed a new class of malonate-derived detergents with four glucosides, designated malonate-derived tetra-glucosides (MTGs), and compared these new detergents with previously reported octyl glucose neopentyl glycol (OGNG) and n-dodecyl-β-d-maltoside (DDM). When tested with two G-protein coupled receptors (GPCRs) and three transporters, a couple of MTGs consistently conferred enhanced stability to all tested proteins compared to DDM and OGNG. As a result of favorable behaviors for a range of membrane proteins, these MTGs have substantial potential for membrane protein research. This study additionally provides a new detergent design principle based on the effect of a polar functional group (i.e., ether) on protein stability depending on its position in the detergent scaffold.
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- 2020
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17. Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody
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Yang, Zhi, Wang, Haoqing, Liu, Albert Z., Gristick, Harry B., and Bjorkman, Pamela J.
- Abstract
The human immunodeficiency virus (HIV-1) envelope (Env) glycoprotein, a (gp120–gp41)3trimer, mediates fusion of viral and host cell membranes after gp120 binding to host receptor CD4. Receptor binding triggers conformational changes allowing coreceptor (CCR5) recognition through CCR5’s tyrosine-sulfated amino (N) terminus, release of the gp41 fusion peptide and fusion. We present 3.3 Å and 3.5 Å cryo-EM structures of E51, a tyrosine-sulfated coreceptor-mimicking antibody, complexed with a CD4-bound open HIV-1 native-like Env trimer. Two classes of asymmetric Env interact with E51, revealing tyrosine-sulfated interactions with gp120 mimicking CCR5 interactions, and two conformations of gp120–gp41 protomers (A and B protomers in AAB and ABB trimers) that differ in their degree of CD4-induced trimer opening and induction of changes to the fusion peptide. By integrating the new structural information with previous closed and open envelope trimer structures, we modeled the order of conformational changes on the path to coreceptor binding site exposure and subsequent viral–host cell membrane fusion.
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- 2019
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18. Immunization expands B cells specific to HIV-1 V3 glycan in mice and macaques
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Escolano, Amelia, Gristick, Harry B., Abernathy, Morgan E., Merkenschlager, Julia, Gautam, Rajeev, Oliveira, Thiago Y., Pai, Joy, West, Anthony P., Barnes, Christopher O., Cohen, Alexander A., Wang, Haoqing, Golijanin, Jovana, Yost, Daniel, Keeffe, Jennifer R., Wang, Zijun, Zhao, Peng, Yao, Kai-Hui, Bauer, Jens, Nogueira, Lilian, Gao, Han, Voll, Alisa V., Montefiori, David C., Seaman, Michael S., Gazumyan, Anna, Silva, Murillo, McGuire, Andrew T., Stamatatos, Leonidas, Irvine, Darrell J., Wells, Lance, Martin, Malcolm A., Bjorkman, Pamela J., and Nussenzweig, Michel C.
- Abstract
Broadly neutralizing monoclonal antibodies protect against infection with HIV-1 in animal models, suggesting that a vaccine that elicits these antibodies would be protective in humans. However, it has not yet been possible to induce adequate serological responses by vaccination. Here, to activate B cells that express precursors of broadly neutralizing antibodies within polyclonal repertoires, we developed an immunogen, RC1, that facilitates the recognition of the variable loop 3 (V3)-glycan patch on the envelope protein of HIV-1. RC1 conceals non-conserved immunodominant regions by the addition of glycans and/or multimerization on virus-like particles. Immunization of mice, rabbits and rhesus macaques with RC1 elicited serological responses that targeted the V3-glycan patch. Antibody cloning and cryo-electron microscopy structures of antibody–envelope complexes confirmed that immunization with RC1 expands clones of B cells that carry the anti-V3-glycan patch antibodies, which resemble precursors of human broadly neutralizing antibodies. Thus, RC1 may be a suitable priming immunogen for sequential vaccination strategies in the context of polyclonal repertoires.
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- 2019
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19. Inside Back Cover: Biomembrane force probe (BFP): Design, advancements, and recent applications to live‐cell mechanobiology (EXP2 4/2023)
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Moldovan, Laura, Song, Caroline Haoran, Chen, Yiyao Catherine, Wang, Haoqing Jerry, and Ju, Lining Arnold
- Abstract
The cover image encapsulates the core principles of a robust technique known as the biomembrane force probe (BFP). It visually portrays the application of BFP in investigating single‐cell interactions, particularly in the context of circulation. The image showcases the intricate design of the BFP apparatus employing a T‐cell as a representative model, and emphasizes its ability to probe molecular interactions.
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- 2023
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20. Biomembrane force probe (BFP): Design, advancements, and recent applications to live‐cell mechanobiology
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Moldovan, Laura, Song, Caroline Haoran, Chen, Yiyao Catherine, Wang, Haoqing Jerry, and Ju, Lining Arnold
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Mechanical forces play a vital role in biological processes at molecular and cellular levels, significantly impacting various diseases such as cancer, cardiovascular disease, and COVID‐19. Recent advancements in dynamic force spectroscopy (DFS) techniques have enabled the application and measurement of forces and displacements with high resolutions, providing crucial insights into the mechanical pathways underlying these diseases. Among DFS techniques, the biomembrane force probe (BFP) stands out for its ability to measure bond kinetics and cellular mechanosensing with pico‐newton and nano‐meter resolutions. Here, a comprehensive overview of the classical BFP‐DFS setup is presented and key advancements are emphasized, including the development of dual biomembrane force probe (dBFP) and fluorescence biomembrane force probe (fBFP). BFP‐DFS allows us to investigate dynamic bond behaviors on living cells and significantly enhances the understanding of specific ligand‐receptor axes mediated cell mechanosensing. The contributions of BFP‐DFS to the fields of cancer biology, thrombosis, and inflammation are delved into, exploring its potential to elucidate novel therapeutic discoveries. Furthermore, future BFP upgrades aimed at improving output and feasibility are anticipated, emphasizing its growing importance in the field of cell mechanobiology. Although BFP‐DFS remains a niche research modality, its impact on the expanding field of cell mechanobiology is immense. This review provides a thorough examination of the traditional BFP‐DFS configurations, highlighting notable progressions such as the introduction of the dual biomembrane force probe (dBFP) and the fluorescence biomembrane force probe (fBFP). The significant contributions of the BFP‐DFS to cancer biology, thrombosis, and inflammation are explored, underscoring its potential for unveiling therapeutic insights. Additionally, forthcoming enhancements to the BFP technology that aim to enhance its output and feasibility are anticipated, thereby emphasizing its increasing significance in the realm of cell mechanobiology.
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- 2023
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21. Negative allosteric modulation of the glucagon receptor by RAMP2
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O'Brien, Evan S., Krishna Kumar, Kaavya, Habrian, Chris, Latorraca, Naomi R., Wang, Haoqing, Tuneew, Inga, Montabana, Elizabeth, Marqusee, Susan, Hilger, Daniel, Isacoff, Ehud Y., Mathiesen, Jesper M., and Kobilka, Brian K.
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- 2023
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22. Sequential immunization of macaques elicits heterologous neutralizing antibodies targeting the V3-glycan patch of HIV-1 Env
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Escolano, Amelia, Gristick, Harry B., Gautam, Rajeev, DeLaitsch, Andrew T., Abernathy, Morgan E., Yang, Zhi, Wang, Haoqing, Hoffmann, Magnus A.G., Nishimura, Yoshiaki, Wang, Zijun, Koranda, Nicholas, Kakutani, Leesa M., Gao, Han, Gnanapragasam, Priyanthi N. P., Raina, Henna, Gazumyan, Ana, Cipolla, Melissa, Oliveira, Thiago Y., Ramos, Victor, Irvine, Darrell J., Silva, Murillo, West, Anthony P., Keeffe, Jennifer R., Barnes, Christopher O., Seaman, Michael S., Nussenzweig, Michel C., Martin, Malcolm A., and Bjorkman, Pamela J.
- Abstract
Description
- Published
- 2021
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23. Publisher Correction: Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody
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Yang, Zhi, Wang, Haoqing, Liu, Albert Z., Gristick, Harry B., and Bjorkman, Pamela J.
- Abstract
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
- Published
- 2020
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24. Publisher Correction: Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody
- Author
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Yang, Zhi, Wang, Haoqing, Liu, Albert Z., Gristick, Harry B., and Bjorkman, Pamela J.
- Abstract
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
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- 2020
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25. Coexistence of potent HIV-1 broadly neutralizing antibodies and antibody-sensitive viruses in a viremic controller
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Freund, Natalia T., Wang, Haoqing, Scharf, Louise, Nogueira, Lilian, Horwitz, Joshua A., Bar-On, Yotam, Golijanin, Jovana, Sievers, Stuart A., Sok, Devin, Cai, Hui, Cesar Lorenzi, Julio C., Halper-Stromberg, Ariel, Toth, Ildiko, Piechocka-Trocha, Alicja, Gristick, Harry B., van Gils, Marit J., Sanders, Rogier W., Wang, Lai-Xi, Seaman, Michael S., Burton, Dennis R., Gazumyan, Anna, Walker, Bruce D., West, Anthony P., Bjorkman, Pamela J., and Nussenzweig, Michel C.
- Abstract
Three new potent neutralizing antibodies neutralize autologous HIV-1 strains and contribute to viral control in an HIV-1 controller.
- Published
- 2017
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