Scholars@Duke

• Background
• 

  Education, Training, & Certifications

  • Ph.D., Centre for Cellular and Molecular Biology (India) 2003
  • M.S., Jadavpur University (India) 1996
  • B.S., Jadavpur University (India) 1994
• 

  Previous Appointments & Affiliations

  • Associate Professor in Surgery, Surgery, Surgical Sciences, Surgery 2018 - 2019
  • Instructor in the Department of Surgery, Surgery, Surgical Sciences, Surgery 2018
• Recognition
• 

  In the News

  • JUN 28, 2022

    Duke Health News

    Duke Awarded Federal Grant to Build Structural Models of HIV

  • JUN 29, 2021

    Duke Health News

    Duke Researchers Point to Protein Spike as the Key to SARS Viral Variations & Increased Transmission

  • MAY 20, 2021

    Duke Health News

    Newly Identified Antibody Can Be Targeted by HIV Vaccines

  • NOV 6, 2020

    School of Medicine

    Years in the Making: Duke Human Vaccine Institute Researchers Attack COVID-19

  • MAR 27, 2020

    Duke University School of Medicine

    Duke Leverages Cryo-Electron Microscope Facility in the Race for Coronavirus Vaccine

  • JAN 31, 2020

    Creating a Vaccine to Guide the Immune System to Make the Right Kind of Antibodies
• Research
• 

  Selected Grants

  • SOSIP-NP/mRNA combination for novel preventive and therapeutic HIV-1 vaccine regimens awarded by National Institutes of Health 2022 - 2027
  • Duke Center for HIV Structural Biology awarded by National Institutes of Health 2022 - 2027
  • Structural and biophysical studies on natural SARS-CoV-2 variants awarded by National Institutes of Health 2022 - 2027
  • Structural characterization of Fab-dimerized glycan-reactive antibodies that neutralize HIV-1 awarded by National Institutes of Health 2021 - 2026
  • Interdisciplinary Research Training Program in AIDS awarded by National Institutes of Health 2010 - 2025
  • HIV-1 vaccine-elicited antibodies target envelope glycans awarded by National Institutes of Health 2015 - 2025
  • Structures of initial CD4 engagement with pre-fusion, closed HIV-1 Envelope trimer and early CD4-induced conformational changes required for infection awarded by National Institutes of Health 2019 - 2024
  • Dissecting the mechanisms of HIV resistance in vivo to broadly neutralizing antibodies awarded by University of Minnesota 2022 - 2023
  • SHIV/HIV Env-antibody coevolution as a molecular guide to V3 glycan targeted vaccine design awarded by University of Pennsylvania 2022 - 2023
  • Structure, dynamics and evolution of the HIV-1 Phe-43 cavity awarded by National Institutes of Health 2020 - 2022
  • GH-VAP: Duke Antibody Dynamics Core Extension; INV-008612 Supplement awarded by Bill and Melinda Gates Foundation 2019 - 2022
  • Coronavirus Vaccine Design awarded by State of North Carolina 2020 - 2021
  • Studying the effect on HIV-1 Env structure and immune response to HIV-1 infection in mucosal fluids using Negative Stain Electron Microscopy awarded by Fred Hutchinson Cancer Research Center 2018 - 2019
• Publications & Artistic Works
• 

  Selected Publications

  • Academic Articles

    • Henderson, Rory, Ye Zhou, Victoria Stalls, Kevin Wiehe, Kevin O. Saunders, Kshitij Wagh, Kara Anasti, et al. “Structural basis for breadth development in the HIV-1 V3-glycan targeting DH270 antibody clonal lineage.” Nat Commun 14, no. 1 (May 15, 2023): 2782. https://doi.org/10.1038/s41467-023-38108-1.
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    • Bennett, A. L., C. Saunders, Y. Bililign, A. Williams, M. Montani, P. Acharya, B. Haynes, and R. C. Henderson. “Examining HIV-1 envelope conformational transitions at high temporal resolution.” Biophysical Journal 122, no. 3S1 (February 10, 2023): 188a-189a. https://doi.org/10.1016/j.bpj.2022.11.1158.
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    • Wrapp, Daniel, Zekun Mu, Bhishem Thakur, Katarzyna Janowska, Oluwatobi Ajayi, Maggie Barr, Robert Parks, et al. “Structure-Based Stabilization of SOSIP Env Enhances Recombinant Ectodomain Durability and Yield.” J Virol 97, no. 1 (January 31, 2023): e0167322. https://doi.org/10.1128/jvi.01673-22.
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    • Pilewski, Kelsey A., Steven Wall, Simone I. Richardson, Nelia P. Manamela, Kaitlyn Clark, Tandile Hermanus, Elad Binshtein, et al. “Functional HIV-1/HCV cross-reactive antibodies isolated from a chronically co-infected donor.” Cell Rep 42, no. 2 (January 27, 2023): 112044. https://doi.org/10.1016/j.celrep.2023.112044.
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    • Manrique, Pedro D., Srirupa Chakraborty, Rory Henderson, Robert J. Edwards, Rachael Mansbach, Kien Nguyen, Victoria Stalls, et al. “Network analysis uncovers the communication structure of SARS-CoV-2 spike protein identifying sites for immunogen design.” Iscience 26, no. 1 (January 20, 2023): 105855. https://doi.org/10.1016/j.isci.2022.105855.
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    • Stalls, Victoria, Katarzyna Janowska, and Priyamvada Acharya. “Transient transfection and purification of SARS-CoV-2 spike protein from mammalian cells.” Star Protoc 3, no. 3 (September 16, 2022): 101603. https://doi.org/10.1016/j.xpro.2022.101603.
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    • Saunders, Kevin O., Robert J. Edwards, Kedamawit Tilahun, Kartik Manne, Xiaozhi Lu, Derek W. Cain, Kevin Wiehe, et al. “Stabilized HIV-1 envelope immunization induces neutralizing antibodies to the CD4bs and protects macaques against mucosal infection.” Sci Transl Med 14, no. 661 (September 7, 2022): eabo5598. https://doi.org/10.1126/scitranslmed.abo5598.
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    • Stalls, Victoria, Jared Lindenberger, Sophie M-C Gobeil, Rory Henderson, Rob Parks, Maggie Barr, Margaret Deyton, et al. “Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike.” Cell Rep 39, no. 13 (June 28, 2022): 111009. https://doi.org/10.1016/j.celrep.2022.111009.
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    • Gobeil, Sophie M-C, Rory Henderson, Victoria Stalls, Katarzyna Janowska, Xiao Huang, Aaron May, Micah Speakman, et al. “Structural diversity of the SARS-CoV-2 Omicron spike.” Mol Cell 82, no. 11 (June 2, 2022): 2050-2068.e6. https://doi.org/10.1016/j.molcel.2022.03.028.
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    • Li, Dapeng, Gregory D. Sempowski, Kevin O. Saunders, Priyamvada Acharya, and Barton F. Haynes. “SARS-CoV-2 Neutralizing Antibodies for COVID-19 Prevention and Treatment.” Annu Rev Med 73 (January 27, 2022): 1–16. https://doi.org/10.1146/annurev-med-042420-113838.
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    • Martinez, David R., Alexandra Schäfer, Sophie Gobeil, Dapeng Li, Gabriela De la Cruz, Robert Parks, Xiaozhi Lu, et al. “A broadly cross-reactive antibody neutralizes and protects against sarbecovirus challenge in mice.” Sci Transl Med 14, no. 629 (January 26, 2022): eabj7125. https://doi.org/10.1126/scitranslmed.abj7125.
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    • Murji, Amyn A., Nagarajan Raju, Juliana S. Qin, Haajira Kaldine, Katarzyna Janowska, Emilee Friedman Fechter, Rutendo Mapengo, et al. “Sequence and functional characterization of a public HIV-specific antibody clonotype.” Iscience 25, no. 1 (January 21, 2022): 103564. https://doi.org/10.1016/j.isci.2021.103564.
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    • Stalls, Victoria, and Priyamvada Acharya. “How to train your antibody to fight malaria.” Immunity 54, no. 12 (December 14, 2021): 2692–94. https://doi.org/10.1016/j.immuni.2021.11.007.
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    • Cottrell, Christopher A., Kartik Manne, Rui Kong, Shuishu Wang, Tongqing Zhou, Gwo-Yu Chuang, Robert J. Edwards, et al. “Structural basis of glycan276-dependent recognition by HIV-1 broadly neutralizing antibodies.” Cell Reports 37, no. 5 (November 2021): 109922. https://doi.org/10.1016/j.celrep.2021.109922.
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    • Li, Dapeng, Robert J. Edwards, Kartik Manne, David R. Martinez, Alexandra Schäfer, S Munir Alam, Kevin Wiehe, et al. “In vitro and in vivo functions of SARS-CoV-2 infection-enhancing and neutralizing antibodies.” Cell 184, no. 16 (August 5, 2021): 4203-4219.e32. https://doi.org/10.1016/j.cell.2021.06.021.
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    • Gobeil, Sophie M-C, Katarzyna Janowska, Shana McDowell, Katayoun Mansouri, Robert Parks, Victoria Stalls, Megan F. Kopp, et al. “Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity.” Science (New York, N.Y.) 373, no. 6555 (August 2021): eabi6226. https://doi.org/10.1126/science.abi6226.
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    • Montefiori, David C., and Priyamvada Acharya. “SnapShot: SARS-CoV-2 antibodies.” Cell Host Microbe 29, no. 7 (July 14, 2021): 1162-1162.e1. https://doi.org/10.1016/j.chom.2021.06.005.
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    • Shiakolas, Andrea R., Kevin J. Kramer, Daniel Wrapp, Simone I. Richardson, Alexandra Schäfer, Steven Wall, Nianshuang Wang, et al. “Cross-reactive coronavirus antibodies with diverse epitope specificities and Fc effector functions.” Cell Rep Med 2, no. 6 (June 15, 2021): 100313. https://doi.org/10.1016/j.xcrm.2021.100313.
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    • Saunders, Kevin O., Esther Lee, Robert Parks, David R. Martinez, Dapeng Li, Haiyan Chen, Robert J. Edwards, et al. “Neutralizing antibody vaccine for pandemic and pre-emergent coronaviruses.” Nature 594, no. 7864 (June 2021): 553–59. https://doi.org/10.1038/s41586-021-03594-0.
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    • Williams, Wilton B., R Ryan Meyerhoff, R. J. Edwards, Hui Li, Kartik Manne, Nathan I. Nicely, Rory Henderson, et al. “Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies.” Cell 184, no. 11 (May 27, 2021): 2955-2972.e25. https://doi.org/10.1016/j.cell.2021.04.042.
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    • Parker, Robert, Thomas Partridge, Catherine Wormald, Rebeca Kawahara, Victoria Stalls, Maria Aggelakopoulou, Jimmy Parker, et al. “Mapping the SARS-CoV-2 spike glycoprotein-derived peptidome presented by HLA class II on dendritic cells.” Cell Rep 35, no. 8 (May 25, 2021): 109179. https://doi.org/10.1016/j.celrep.2021.109179.
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    • Martinez, David R., Alexandra Schaefer, Sophie Gobeil, Dapeng Li, Gabriela De la Cruz, Robert Parks, Xiaozhi Lu, et al. “A broadly neutralizing antibody protects against SARS-CoV, pre-emergent bat CoVs, and SARS-CoV-2 variants in mice.” Biorxiv, April 28, 2021. https://doi.org/10.1101/2021.04.27.441655.
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    • Gobeil, Sophie M-C, Katarzyna Janowska, Shana McDowell, Katayoun Mansouri, Robert Parks, Victoria Stalls, Megan F. Kopp, et al. “Effect of natural mutations of SARS-CoV-2 on spike structure, conformation and antigenicity.” Biorxiv, March 15, 2021. https://doi.org/10.1101/2021.03.11.435037.
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    • Li, Dapeng, Robert J. Edwards, Kartik Manne, David R. Martinez, Alexandra Schäfer, S Munir Alam, Kevin Wiehe, et al. “The functions of SARS-CoV-2 neutralizing and infection-enhancing antibodies in vitro and in mice and nonhuman primates.” Biorxiv, February 18, 2021. https://doi.org/10.1101/2020.12.31.424729.
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    • Saunders, Kevin O., Esther Lee, Robert Parks, David R. Martinez, Dapeng Li, Haiyan Chen, Robert J. Edwards, et al. “SARS-CoV-2 vaccination induces neutralizing antibodies against pandemic and pre-emergent SARS-related coronaviruses in monkeys.” Biorxiv, February 17, 2021. https://doi.org/10.1101/2021.02.17.431492.
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    • Edwards, Robert J., Katayoun Mansouri, Victoria Stalls, Kartik Manne, Brian Watts, Rob Parks, Katarzyna Janowska, et al. “Cold sensitivity of the SARS-CoV-2 spike ectodomain.” Nat Struct Mol Biol 28, no. 2 (February 2021): 128–31. https://doi.org/10.1038/s41594-020-00547-5.
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    • Weissman, Drew, Mohamad-Gabriel Alameh, Thushan de Silva, Paul Collini, Hailey Hornsby, Rebecca Brown, Celia C. LaBranche, et al. “D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization.” Cell Host Microbe 29, no. 1 (January 13, 2021): 23-31.e4. https://doi.org/10.1016/j.chom.2020.11.012.
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    • Gobeil, Sophie M-C, Katarzyna Janowska, Shana McDowell, Katayoun Mansouri, Robert Parks, Kartik Manne, Victoria Stalls, et al. “D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction.” Cell Rep 34, no. 2 (January 12, 2021): 108630. https://doi.org/10.1016/j.celrep.2020.108630.
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    • Nyanhete, Tinashe E., Robert J. Edwards, Celia C. LaBranche, Katayoun Mansouri, Amanda Eaton, S Moses Dennison, Kevin O. Saunders, et al. “Polyclonal Broadly Neutralizing Antibody Activity Characterized by CD4 Binding Site and V3-Glycan Antibodies in a Subset of HIV-1 Virus Controllers.” Front Immunol 12 (2021): 670561. https://doi.org/10.3389/fimmu.2021.670561.
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    • Edwards, Robert J., Katayoun Mansouri, Victoria Stalls, Kartik Manne, Brian Watts, Rob Parks, Katarzyna Janowska, et al. “Cold sensitivity of the SARS-CoV-2 spike ectodomain.” Biorxiv, October 13, 2020. https://doi.org/10.1101/2020.07.12.199588.
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    • Gobeil, Sophie, Katarzyna Janowska, Shana McDowell, Katayoun Mansouri, Robert Parks, Kartik Manne, Victoria Stalls, et al. “D614G mutation alters SARS-CoV-2 spike conformational dynamics and protease cleavage susceptibility at the S1/S2 junction.” Biorxiv, October 12, 2020. https://doi.org/10.1101/2020.10.11.335299.
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    • Henderson, Rory, Robert J. Edwards, Katayoun Mansouri, Katarzyna Janowska, Victoria Stalls, Sophie M. C. Gobeil, Megan Kopp, et al. “Controlling the SARS-CoV-2 spike glycoprotein conformation.” Nat Struct Mol Biol 27, no. 10 (October 2020): 925–33. https://doi.org/10.1038/s41594-020-0479-4.
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    • Sempowski, Gregory D., Kevin O. Saunders, Priyamvada Acharya, Kevin J. Wiehe, and Barton F. Haynes. “Pandemic Preparedness: Developing Vaccines and Therapeutic Antibodies For COVID-19.” Cell 181, no. 7 (June 2020): 1458–63. https://doi.org/10.1016/j.cell.2020.05.041.
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    • Henderson, Rory, Robert J. Edwards, Katayoun Mansouri, Katarzyna Janowska, Victoria Stalls, Sophie Gobeil, Megan Kopp, et al. “Controlling the SARS-CoV-2 Spike Glycoprotein Conformation.” Biorxiv, May 18, 2020. https://doi.org/10.1101/2020.05.18.102087.
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    • Henderson, Rory, Maolin Lu, Ye Zhou, Zekun Mu, Robert Parks, Qifeng Han, Allen L. Hsu, et al. “Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements.” Nat Commun 11, no. 1 (January 24, 2020): 520. https://doi.org/10.1038/s41467-019-14196-w.
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    • Acharya, P., R. Edwards, R. Henderson, K. Manne, K. Mansouri, K. Janowska, S. McDowell, V. Stalls, M. Kopp, and B. Haynes. “How does HIV env structure informs vaccine design?” Microscopy and Microanalysis, January 1, 2020. https://doi.org/10.1017/S1431927620015135.
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    • Setliff, Ian, Andrea R. Shiakolas, Kelsey A. Pilewski, Amyn A. Murji, Rutendo E. Mapengo, Katarzyna Janowska, Simone Richardson, et al. “High-Throughput Mapping of B Cell Receptor Sequences to Antigen Specificity.” Cell 179, no. 7 (December 12, 2019): 1636-1646.e15. https://doi.org/10.1016/j.cell.2019.11.003.
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    • Saunders, Kevin O., Kevin Wiehe, Ming Tian, Priyamvada Acharya, Todd Bradley, S Munir Alam, Eden P. Go, et al. “Targeted selection of HIV-specific antibody mutations by engineering B cell maturation.” Science 366, no. 6470 (December 6, 2019). https://doi.org/10.1126/science.aay7199.
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    • LaBranche, Celia C., Rory Henderson, Allen Hsu, Shay Behrens, Xuejun Chen, Tongqing Zhou, Kevin Wiehe, et al. “Correction: Neutralization-guided design of HIV-1 envelope trimers with high affinity for the unmutated common ancestor of CH235 lineage CD4bs broadly neutralizing antibodies.” Plos Pathog 15, no. 12 (December 2019): e1008200. https://doi.org/10.1371/journal.ppat.1008200.
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    • LaBranche, Celia C., Rory Henderson, Allen Hsu, Shay Behrens, Xuejun Chen, Tongqing Zhou, Kevin Wiehe, et al. “Neutralization-guided design of HIV-1 envelope trimers with high affinity for the unmutated common ancestor of CH235 lineage CD4bs broadly neutralizing antibodies.” Plos Pathog 15, no. 9 (September 2019): e1008026. https://doi.org/10.1371/journal.ppat.1008026.
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    • Kong, Rui, Hongying Duan, Zizhang Sheng, Kai Xu, Priyamvada Acharya, Xuejun Chen, Cheng Cheng, et al. “Antibody Lineages with Vaccine-Induced Antigen-Binding Hotspots Develop Broad HIV Neutralization.” Cell 178, no. 3 (July 25, 2019): 567-584.e19. https://doi.org/10.1016/j.cell.2019.06.030.
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    • Chuang, Gwo-Yu, Jing Zhou, Priyamvada Acharya, Reda Rawi, Chen-Hsiang Shen, Zizhang Sheng, Baoshan Zhang, et al. “Structural Survey of Broadly Neutralizing Antibodies Targeting the HIV-1 Env Trimer Delineates Epitope Categories and Characteristics of Recognition.” Structure 27, no. 1 (January 2, 2019): 196-206.e6. https://doi.org/10.1016/j.str.2018.10.007.
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    • Stewart-Jones, Guillaume B. E., Gwo-Yu Chuang, Kai Xu, Tongqing Zhou, Priyamvada Acharya, Yaroslav Tsybovsky, Li Ou, et al. “Structure-based design of a quadrivalent fusion glycoprotein vaccine for human parainfluenza virus types 1-4.” Proc Natl Acad Sci U S A 115, no. 48 (November 27, 2018): 12265–70. https://doi.org/10.1073/pnas.1811980115.
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    • Dingens, Adam S., Priyamvada Acharya, Hugh K. Haddox, Reda Rawi, Kai Xu, Gwo-Yu Chuang, Hui Wei, et al. “Complete functional mapping of infection- and vaccine-elicited antibodies against the fusion peptide of HIV.” Plos Pathog 14, no. 7 (July 2018): e1007159. https://doi.org/10.1371/journal.ppat.1007159.
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    • Xu, Kai, Priyamvada Acharya, Rui Kong, Cheng Cheng, Gwo-Yu Chuang, Kevin Liu, Mark K. Louder, et al. “Epitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1.” Nat Med 24, no. 6 (June 2018): 857–67. https://doi.org/10.1038/s41591-018-0042-6.
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    • Noble, Alex J., Venkata P. Dandey, Hui Wei, Julia Brasch, Jillian Chase, Priyamvada Acharya, Yong Zi Tan, et al. “Routine single particle CryoEM sample and grid characterization by tomography.” Elife 7 (May 29, 2018). https://doi.org/10.7554/eLife.34257.
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    • Georgiev, Ivelin S., Michael Gordon Joyce, Rita E. Chen, Kwanyee Leung, Krisha McKee, Aliaksandr Druz, Joseph G. Van Galen, et al. “Two-Component Ferritin Nanoparticles for Multimerization of Diverse Trimeric Antigens.” Acs Infect Dis 4, no. 5 (May 11, 2018): 788–96. https://doi.org/10.1021/acsinfecdis.7b00192.
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    • Dandey, Venkata P., Hui Wei, Zhening Zhang, Yong Zi Tan, Priyamvada Acharya, Edward T. Eng, William J. Rice, Peter A. Kahn, Clinton S. Potter, and Bridget Carragher. “Spotiton: New features and applications.” J Struct Biol 202, no. 2 (May 2018): 161–69. https://doi.org/10.1016/j.jsb.2018.01.002.
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    • Chuang, Gwo-Yu, Hui Geng, Marie Pancera, Kai Xu, Cheng Cheng, Priyamvada Acharya, Michael Chambers, et al. “Structure-Based Design of a Soluble Prefusion-Closed HIV-1 Env Trimer with Reduced CD4 Affinity and Improved Immunogenicity.” J Virol 91, no. 10 (May 15, 2017). https://doi.org/10.1128/JVI.02268-16.
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    • Liu, Qingbo, Priyamvada Acharya, Michael A. Dolan, Peng Zhang, Christina Guzzo, Jacky Lu, Alice Kwon, et al. “Quaternary contact in the initial interaction of CD4 with the HIV-1 envelope trimer.” Nat Struct Mol Biol 24, no. 4 (April 2017): 370–78. https://doi.org/10.1038/nsmb.3382.
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    • Kong, Rui, Kai Xu, Tongqing Zhou, Priyamvada Acharya, Thomas Lemmin, Kevin Liu, Gabriel Ozorowski, et al. “Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.” Science 352, no. 6287 (May 13, 2016): 828–33. https://doi.org/10.1126/science.aae0474.
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    • Bonsignori, Mattia, Tongqing Zhou, Zizhang Sheng, Lei Chen, Feng Gao, M Gordon Joyce, Gabriel Ozorowski, et al. “Maturation Pathway from Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody.” Cell 165, no. 2 (April 7, 2016): 449–63. https://doi.org/10.1016/j.cell.2016.02.022.
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    • Gohain, Neelakshi, William D. Tolbert, Priyamvada Acharya, Lei Yu, Tongyun Liu, Pingsen Zhao, Chiara Orlandi, et al. “Cocrystal Structures of Antibody N60-i3 and Antibody JR4 in Complex with gp120 Define More Cluster A Epitopes Involved in Effective Antibody-Dependent Effector Function against HIV-1.” J Virol 89, no. 17 (September 2015): 8840–54. https://doi.org/10.1128/JVI.01232-15.
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    • Kwon, Young Do, Marie Pancera, Priyamvada Acharya, Ivelin S. Georgiev, Emma T. Crooks, Jason Gorman, M Gordon Joyce, et al. “Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env.” Nat Struct Mol Biol 22, no. 7 (July 2015): 522–31. https://doi.org/10.1038/nsmb.3051.
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    • Zhou, Tongqing, Rebecca M. Lynch, Lei Chen, Priyamvada Acharya, Xueling Wu, Nicole A. Doria-Rose, M Gordon Joyce, et al. “Structural Repertoire of HIV-1-Neutralizing Antibodies Targeting the CD4 Supersite in 14 Donors.” Cell 161, no. 6 (June 4, 2015): 1280–92. https://doi.org/10.1016/j.cell.2015.05.007.
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    • Acharya, Priyamvada, Sabrina Lusvarghi, Carole A. Bewley, and Peter D. Kwong. “HIV-1 gp120 as a therapeutic target: navigating a moving labyrinth.” Expert Opin Ther Targets 19, no. 6 (June 2015): 765–83. https://doi.org/10.1517/14728222.2015.1010513.
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    • Shingai, Masashi, Sarah Welbourn, Jason M. Brenchley, Priyamvada Acharya, Eri Miyagi, Ronald J. Plishka, Alicia Buckler-White, et al. “The Expression of Functional Vpx during Pathogenic SIVmac Infections of Rhesus Macaques Suppresses SAMHD1 in CD4+ Memory T Cells.” Plos Pathog 11, no. 5 (May 2015): e1004928. https://doi.org/10.1371/journal.ppat.1004928.
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    • Barbian, Hannah J., Julie M. Decker, Frederic Bibollet-Ruche, Rachel P. Galimidi, Anthony P. West, Gerald H. Learn, Nicholas F. Parrish, et al. “Neutralization properties of simian immunodeficiency viruses infecting chimpanzees and gorillas.” Mbio 6, no. 2 (April 21, 2015). https://doi.org/10.1128/mBio.00296-15.
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    • Acharya, P., T. S. Luongo, I. S. Georgiev, J. Matz, S. D. Schmidt, M. K. Louder, P. Kessler, et al. “Correction to Heavy Chain-Only IgG2b Llama antibody effects Near-Pan HIV-1 neutralization by recognizing a CD4-induced epitope that includes elements of coreceptor- and CD4-binding sites [Journal of Virology 87, 18, (2013) 10173-10181].” Journal of Virology 89, no. 1 (January 1, 2015): 883–85. https://doi.org/10.1128/JVI.02621-14.
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    • Acharya, Priyamvada, William D. Tolbert, Neelakshi Gohain, Xueji Wu, Lei Yu, Tongyun Liu, Wensheng Huang, et al. “Structural definition of an antibody-dependent cellular cytotoxicity response implicated in reduced risk for HIV-1 infection.” J Virol 88, no. 21 (November 2014): 12895–906. https://doi.org/10.1128/JVI.02194-14.
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    • Pancera, Marie, Tongqing Zhou, Aliaksandr Druz, Ivelin S. Georgiev, Cinque Soto, Jason Gorman, Jinghe Huang, et al. “Structure and immune recognition of trimeric pre-fusion HIV-1 Env.” Nature 514, no. 7523 (October 23, 2014): 455–61. https://doi.org/10.1038/nature13808.
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    • Acharya, Priyamvada, Timothy S. Luongo, Ivelin S. Georgiev, Julie Matz, Stephen D. Schmidt, Mark K. Louder, Pascal Kessler, et al. “Heavy chain-only IgG2b llama antibody effects near-pan HIV-1 neutralization by recognizing a CD4-induced epitope that includes elements of coreceptor- and CD4-binding sites.” J Virol 87, no. 18 (September 2013): 10173–81. https://doi.org/10.1128/JVI.01332-13.
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    • Chuang, Gwo-Yu, Priyamvada Acharya, Stephen D. Schmidt, Yongping Yang, Mark K. Louder, Tongqing Zhou, Young Do Kwon, et al. “Residue-level prediction of HIV-1 antibody epitopes based on neutralization of diverse viral strains.” J Virol 87, no. 18 (September 2013): 10047–58. https://doi.org/10.1128/JVI.00984-13.
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    • Zhou, Tongqing, Jiang Zhu, Xueling Wu, Stephanie Moquin, Baoshan Zhang, Priyamvada Acharya, Ivelin S. Georgiev, et al. “Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies.” Immunity 39, no. 2 (August 22, 2013): 245–58. https://doi.org/10.1016/j.immuni.2013.04.012.
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    • Morellato-Castillo, Laurence, Priyamvada Acharya, Olivier Combes, Johan Michiels, Anne Descours, Oscar H. P. Ramos, Yongping Yang, et al. “Interfacial cavity filling to optimize CD4-mimetic miniprotein interactions with HIV-1 surface glycoprotein.” J Med Chem 56, no. 12 (June 27, 2013): 5033–47. https://doi.org/10.1021/jm4002988.
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    • Acharya, Priyamvada, Timothy S. Luongo, Mark K. Louder, Krisha McKee, Yongping Yang, Young Do Kwon, John R. Mascola, Pascal Kessler, Loïc Martin, and Peter D. Kwong. “Structural basis for highly effective HIV-1 neutralization by CD4-mimetic miniproteins revealed by 1.5 Å cocrystal structure of gp120 and M48U1.” Structure 21, no. 6 (June 4, 2013): 1018–29. https://doi.org/10.1016/j.str.2013.04.015.
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    • Georgiev, I., P. Acharya, S. D. Schmidt, Y. Li, D. Wycuff, G. Ofek, N. Doria-Rose, et al. “Design of epitope-specific probes for sera analysis and antibody isolation.” Retrovirology 9 (September 13, 2012).
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    • Dogo-Isonagie, Cajetan, Son Lam, Elena Gustchina, Priyamvada Acharya, Yongping Yang, Syed Shahzad-ul-Hussan, G Marius Clore, Peter D. Kwong, and Carole A. Bewley. “Peptides from second extracellular loop of C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1.” J Biol Chem 287, no. 18 (April 27, 2012): 15076–86. https://doi.org/10.1074/jbc.M111.332361.
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    • Acharya, Priyamvada, Cajetan Dogo-Isonagie, Judith M. LaLonde, Son N. Lam, George J. Leslie, Mark K. Louder, Leah L. Frye, et al. “Structure-based identification and neutralization mechanism of tyrosine sulfate mimetics that inhibit HIV-1 entry.” Acs Chem Biol 6, no. 10 (October 21, 2011): 1069–77. https://doi.org/10.1021/cb200068b.
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    • Lam, Son N., Priyamvada Acharya, Richard Wyatt, Peter D. Kwong, and Carole A. Bewley. “Tyrosine-sulfate isosteres of CCR5 N-terminus as tools for studying HIV-1 entry.” Bioorg Med Chem 16, no. 23 (December 1, 2008): 10113–20. https://doi.org/10.1016/j.bmc.2008.10.005.
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    • Rajakumara, Eerappa, Priyamvada Acharya, Shoeb Ahmad, Rajan Sankaranaryanan, and Nalam M. Rao. “Structural basis for the remarkable stability of Bacillus subtilis lipase (Lip A) at low pH.” Biochim Biophys Acta 1784, no. 2 (February 2008): 302–11. https://doi.org/10.1016/j.bbapap.2007.10.012.
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    • Huang, Chih-Chin, Son N. Lam, Priyamvada Acharya, Min Tang, Shi-Hua Xiang, Syed Shahzad-Ul Hussan, Robyn L. Stanfield, et al. “Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4.” Science 317, no. 5846 (September 28, 2007): 1930–34. https://doi.org/10.1126/science.1145373.
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    • Acharya, Priyamvada, Eberhard Warkentin, Ulrich Ermler, Rudolf K. Thauer, and Seigo Shima. “The structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes.” J Mol Biol 357, no. 3 (March 31, 2006): 870–79. https://doi.org/10.1016/j.jmb.2006.01.015.
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    • Eggert, Thorsten, Susanne Aileen Funke, Nalam M. Rao, Priyamvada Acharya, Holger Krumm, Manfred T. Reetz, and Karl-Erich Jaeger. “Multiplex-PCR-based recombination as a novel high-fidelity method for directed evolution.” Chembiochem 6, no. 6 (June 2005): 1062–67. https://doi.org/10.1002/cbic.200400417.
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    • Acharya, Priyamvada, Meike Goenrich, Christoph H. Hagemeier, Ulrike Demmer, Julia A. Vorholt, Rudolf K. Thauer, and Ulrich Ermler. “How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1.” J Biol Chem 280, no. 14 (April 8, 2005): 13712–19. https://doi.org/10.1074/jbc.M412320200.
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    • Acharya, Priyamvada, Eerappa Rajakumara, Rajan Sankaranarayanan, and Nalam M. Rao. “Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase.” J Mol Biol 341, no. 5 (August 27, 2004): 1271–81. https://doi.org/10.1016/j.jmb.2004.06.059.
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    • Rajakumara, Eerappa, Priyamvada Acharya, Shoeb Ahmad, Vellaiah M. Shanmugam, Nalam M. Rao, and Rajan Sankaranarayanan. “Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase.” Acta Crystallogr D Biol Crystallogr 60, no. Pt 1 (January 2004): 160–62. https://doi.org/10.1107/s0907444903024478.
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    • Acharya, Priyamvada, and N Madhusudhana Rao. “Stability studies on a lipase from Bacillus subtilis in guanidinium chloride.” J Protein Chem 22, no. 1 (January 2003): 51–60. https://doi.org/10.1023/a:1023067827678.
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    • Acharya, P., and N. Madhusudhana Rao. “Anomalous ester hydrolysis in mixed micelles of p-nitrophenyloleate-triton X-100 in the presence of guanidinium chloride: Implications in lipase assays.” Langmuir 18, no. 8 (April 16, 2002): 3018–26. https://doi.org/10.1021/la011460o.
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  • Conference Papers

    • Behrens, Shay, Celia C. LaBranche, Tongqing Zhou, Kevin Wiehe, Mattia Bonsignori, Quentin J. Sattentau, Amanda Eaton, et al. “Germline-targeting and Reverse Engineering to Elicit CH235.12 Lineage bNAbs.” In Aids Research and Human Retroviruses, 34:116–116. MARY ANN LIEBERT, INC, 2018.
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    • Williams, Wilton Bryan, R Ryan Meyerhoff, Hui Li, Priyamvada Acharya, Guillaume B. E. Stewart-Jones, Kevin Wiehe, Thomas B. Kepler, et al. “Macaque SHIV Induction of 2G12-like Broadly Neutralizing Antibodies.” In Aids Research and Human Retroviruses, 34:38–38. MARY ANN LIEBERT, INC, 2018.
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  • Preprints

    • Gobeil, Sophie M-C, Rory Henderson, Victoria Stalls, Katarzyna Janowska, Xiao Huang, Aaron May, Micah Speakman, et al. “Structural diversity of the SARS-CoV-2 Omicron spike.,” January 26, 2022. https://doi.org/10.1101/2022.01.25.477784.
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    • Stalls, Victoria, Jared Lindenberger, Sophie M-C Gobeil, Rory Henderson, Rob Parks, Maggie Barr, Margaret Deyton, et al. “Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike.” BioRxiv, 2022. https://doi.org/10.1101/2022.04.07.487528.
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