Cited by 234vaccines and immunoinformatics approachesSARS-CoV-2 and COVID-19 ResearchVirology and Viral Diseases

The DOI matches its Crossref record; 93 of the 94 references it cites were found in a registry or an index.

Structure-Based Vaccine Antigen Design

Open access

Graham, Barney S., Gilman, Morgan S.A., McLellan, Jason S.·2019·Annual Review of Medicine

DOI 10.1146/annurev-med-121217-094234PMC PMC6936610

Open this paper in CoChat — free account

Abstract

Enabled by new approaches for rapid identification and selection of human monoclonal antibodies, atomic-level structural information for viral surface proteins, and capacity for precision engineering of protein immunogens and self-assembling nanoparticles, a new era of antigen design and display options has evolved. While HIV-1 vaccine development has been a driving force behind these technologies and concepts, clinical proof-of-concept for structure-based vaccine design may first be achieved for respiratory syncytial virus (RSV), where conformation-dependent access to neutralization-sensitive epitopes on the fusion glycoprotein determines the capacity to induce potent neutralizing activity. Success with RSV has motivated structure-based stabilization of other class I viral fusion proteins for use as immunogens and demonstrated the importance of structural information for developing vaccines against other viral pathogens, particularly difficult targets that have resisted prior vaccine development efforts. Solving viral surface protein structures also supports rapid vaccine antigen design and application of platform manufacturing approaches for emerging pathogens.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1146/annurev-med-121217-094234

Cites

93 of 93 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The Burden of Respiratory Syncytial Virus Infection in Young Children
Hall, C. B., Weinberg, G. A., Iwane, M. K., Blumkin, A. K., Edwards, K. M., Staat, M. A., Auinger, P., Griffin, M. R., Poehling, K. A., Erdman, D. D., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0804877 · Cited by 2,250
RESPIRATORY SYNCYTIAL VIRUS DISEASE IN INFANTS DESPITE PRIOR ADMINISTRATION OF ANTIGENIC INACTIVATED VACCINE12
KIM, H. W., CANCHOLA, J. G., BRANDT, C. D., PYLES, G., CHANOCK, R. M., JENSEN, K., & PARROTT, R. H. (1969) · American Journal of Epidemiology · doi:10.1093/oxfordjournals.aje.a120955 · Cited by 1,981
Structure of Dengue Virus
Kuhn, R. J., Zhang, W., Rossmann, M. G., Pletnev, S. V., Corver, J., Lenches, E. M., Jones, C. T., Mukhopadhyay, S., Chipman, P. R., Strauss, E. G., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)00660-8 · Cited by 1,565
Risk of Primary Infection and Reinfection With Respiratory Syncytial Virus
Glezen, W. P. (1986) · Archives of Pediatrics and Adolescent Medicine · doi:10.1001/archpedi.1986.02140200053026 · Cited by 1,517
The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
Rey, F. A., Heinz, F. X., Mandl, C. W., Künz, C., & Harrison, S. C. (1995) · Nature · doi:10.1038/375291a0 · Cited by 1,439
A Neutralizing Antibody Selected from Plasma Cells That Binds to Group 1 and Group 2 Influenza A Hemagglutinins
Corti, D., Voss, J., Gamblin, S. J., Codoni, G., Macagno, A., Jarrossay, D., Vachieri, S. G., Pinna, D., Minola, A., Vanzetta, F., et al. (2011) · Science · doi:10.1126/science.1205669 · Cited by 1,203
Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus
McLellan, J. S., Chen, M., Joyce, M. G., Sastry, M., Stewart-Jones, G. B. E., Yang, Y., Zhang, B., Chen, L., Srivatsan, S., Zheng, A., et al. (2013) · Science · doi:10.1126/science.1243283 · Cited by 1,126
Self-citation
Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073
Self-citation
Efficacy of the Herpes Zoster Subunit Vaccine in Adults 70 Years of Age or Older
Cunningham, A. L., Lal, H., Kovac, M., Chlibek, R., Hwang, S.-J., Díez-Domingo, J., Godeaux, O., Levin, M. J., McElhaney, J. E., Puig-Barberà, J., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1603800 · Cited by 1,070
AN EPIDEMIOLOGIC STUDY OF ALTERED CLINICAL REACTIVITY TO RESPIRATORY SYNCYTIAL (RS) VIRUS INFECTION IN CHILDREN PREVIOUSLY VACCINATED WITH AN INACTIVATED RS VIRUS VACCINE
Kapikian, A. Z., MITCHELL, R. H., Chanock, R. M., Shvedoff, R. A., & STEWART, C. E. (1969) · American Journal of Epidemiology · doi:10.1093/oxfordjournals.aje.a120954 · Cited by 1,035

Show all 94 references

Research works printed but not linked: 5

Chanock R, 1957, Am. J. Hyg., 66, 291
Chanock R, 1957, Am. J. Hyg., 66, 281
Graham BS, 2013, Curr. Top Microbiol. Immunol., 372, 391
Glezen WP, 1986, Am. J. Dis. Child, 140, 543
Barik S, 2013, Curr. Top. Microbiol. Immunol., 372, 173

Sorted by citations

An mRNA Vaccine against SARS-CoV-2 — Preliminary Report
Jackson, L. A., Anderson, E. J., Rouphael, N. G., Roberts, P. C., Makhene, M., Coler, R. N., McCullough, M. P., Chappell, J. D., Denison, M. R., Stevens, L. J., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2022483 · Cited by 3,237
Self-citation
SARS-CoV-2 mRNA Vaccine Design Enabled by Prototype Pathogen Preparedness
Corbett, K. S., Edwards, D. K., Leist, S. R., Abiona, O. M., Boyoglu-Barnum, S., Gillespie, R. A., Himansu, S., Schäfer, A., Ziwawo, C. T., DiPiazza, A. T., et al. (2020) · Nature · doi:10.1038/s41586-020-2622-0 · Cited by 1,615
Self-citation
Evaluation of the mRNA-1273 Vaccine against SARS-CoV-2 in Nonhuman Primates
Corbett, K. S., Flynn, B., Foulds, K. E., Francica, J. R., Boyoglu-Barnum, S., Werner, A. P., Flach, B., O’Connell, S., Bock, K. W., Minai, M., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2024671 · Cited by 1,066
Self-citation
Efficacy and Safety of an mRNA-Based RSV PreF Vaccine in Older Adults
Wilson, E. M. P., Goswami, J., Baqui, A. H., Doreski, P. A., Marc, G. P., Zaman, K., Monroy, J., Duncan, C. J. A., Ujiie, M., Rämet, M., et al. (2023) · New England Journal of Medicine · doi:10.1056/nejmoa2307079 · Cited by 544
The SARS-CoV-2 Spike Glycoprotein Biosynthesis, Structure, Function, and Antigenicity: Implications for the Design of Spike-Based Vaccine Immunogens
Duan, L., Zheng, Q., Zhang, H., Niu, Y., Lou, Y., & Wang, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.576622 · Cited by 417
Designing spatial and temporal control of vaccine responses
Roth, G. A., Picece, V. C. T. M., Ou, B. S., Luo, W., Pulendran, B., & Appel, E. A. (2021) · Nature Reviews Materials · doi:10.1038/s41578-021-00372-2 · Cited by 334
A thermostable, closed SARS-CoV-2 spike protein trimer
Xiong, X., Qu, K., Ciazynska, K. A., Hosmillo, M., Carter, A. P., Ebrahimi, S., Ke, Z., Scheres, S. H. W., Bergamaschi, L., Grice, G. L., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0478-5 · Cited by 313
SARS-CoV-2 mRNA Vaccines: Immunological Mechanism and Beyond
Bettini, E., & Locci, M. (2021) · Vaccines · doi:10.3390/vaccines9020147 · Cited by 292
SARS-CoV-2 simulations go exascale to predict dramatic spike opening and cryptic pockets across the proteome
Zimmerman, M. I., Porter, J. R., Ward, M. D., Singh, S., Vithani, N., Meller, A., Mallimadugula, U. L., Kuhn, C. E., Borowsky, J. H., Wiewiora, R., et al. (2021) · Nature Chemistry · doi:10.1038/s41557-021-00707-0 · Cited by 288
Next‐Generation Vaccines: Nanoparticle‐Mediated DNA and mRNA Delivery
Ho, W., Gao, M., Li, F., Li, Z., Zhang, X., & Xu, X. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202001812 · Cited by 261
Controlling timing and location in vaccines
Irvine, D. J., Aung, A., & Silva, M. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.06.019 · Cited by 255
Structurally Resolved SARS-CoV-2 Antibody Shows High Efficacy in Severely Infected Hamsters and Provides a Potent Cocktail Pairing Strategy
Du, S., Cao, Y., Zhu, Q., Yü, P., Qi, F., Wang, G., Du, X., Bao, L., Deng, W., Zhu, H., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.035 · Cited by 238
Rapid Development of SARS-CoV-2 Spike Protein Receptor-Binding Domain Self-Assembled Nanoparticle Vaccine Candidates
Kang, Y.-F., Sun, C., Zhuang, Z., Yuan, R.-Y., Zheng, Q., Li, J.-P., Zhou, P., Chen, X.-C., Liu, Z., Zhang, X., et al. (2021) · ACS Nano · doi:10.1021/acsnano.0c08379 · Cited by 226
A human antibody reveals a conserved site on beta-coronavirus spike proteins and confers protection against SARS-CoV-2 infection
Zhou, P.-P., Yuan, M., Song, G., Beutler, N., Shaabani, N., Huang, D., He, W., Zhu, X., Callaghan, S., Yong, P., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abi9215 · Cited by 196
Opportunities and challenges in design and optimization of protein function
Listov, D., Goverde, C. A., Correia, B. E., & Fleishman, S. J. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00718-y · Cited by 212
Stabilizing the closed SARS-CoV-2 spike trimer
Juraszek, J., Rutten, L., Blokland, S., Bouchier, P., Voorzaat, R., Ritschel, T., Bakkers, M. J. G., Renault, L. L. R., & Langedijk, J. P. M. (2021) · Nature Communications · doi:10.1038/s41467-020-20321-x · Cited by 157
Evaluation of AlphaFold antibody–antigen modeling with implications for improving predictive accuracy
Yin, R., & Pierce, B. G. (2024) · Protein Science · doi:10.1002/pro.4865 · Cited by 145
Computational tools for modern vaccine development
SUNITA, S., Sajid, A., Singh, Y. P., & Shukla, P. (2019) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2019.1670035 · Cited by 141
Vaccines and Therapeutics Against Hantaviruses
Liu, R., Ma, H., Shu, J., Zhang, Q., Han, M., Liu, Z., Jin, X., Zhang, F., & Wu, X. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02989 · Cited by 137
Current Challenges in Vaccinology
Kennedy, R. B., Ovsyannikova, I. G., Palese, P., & Poland, G. A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01181 · Cited by 113
Stopping pandemics before they start: Lessons learned from SARS-CoV-2
Edwards, A. M., Baric, R. S., Saphire, E. O., & Ulmer, J. B. (2022) · Science · doi:10.1126/science.abn1900 · Cited by 109
Development of vaccines and antivirals for combating viral pandemics
Pardi, N., & Weissman, D. (2020) · Nature Biomedical Engineering · doi:10.1038/s41551-020-00658-w · Cited by 108
Virus vaccines: proteins prefer prolines
Sanders, R. W., & Moore, J. P. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.02.002 · Cited by 97
Bottom-up de novo design of functional proteins with complex structural features
Yang, C., Sesterhenn, F., Bonet, J., van Aalen, E. A., Scheller, L., Abriata, L. A., Cramer, J. T., Wen, X., Rosset, S., Georgeon, S., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-020-00699-x · Cited by 84
Low protease activity in B cell follicles promotes retention of intact antigens after immunization
Aung, A., Cui, A., Maiorino, L., Amini, A. P., Gregory, J. R., Bukenya, M., Zhang, Y. J., Lee, H., Cottrell, C. A., Morgan, D. M., et al. (2023) · Science · doi:10.1126/science.abn8934 · Cited by 92
Multivalent antigen display on nanoparticle immunogens increases B cell clonotype diversity and neutralization breadth to pneumoviruses
Ols, S., Lenart, K., Cerveira, R. A., Miranda, M. C., Brunette, N., Kochmann, J., Corcoran, M., Skotheim, R., Philomin, A., Cagigi, A., et al. (2023) · Immunity · doi:10.1016/j.immuni.2023.08.011 · Cited by 80
Self-citation
Advanced technologies for the development of infectious disease vaccines
Gupta, A., Rudra, A., Reed, K., Langer, R., & Anderson, D. G. (2024) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01041-z · Cited by 87
Immunoinformatic design of a COVID-19 subunit vaccine using entire structural immunogenic epitopes of SARS-CoV-2
Behmard, E., Soleymani, B., Najafi, A., & Barzegari, E. (2020) · Scientific Reports · doi:10.1038/s41598-020-77547-4 · Cited by 77
Structure-based design of stabilized recombinant influenza neuraminidase tetramers
Ellis, D., Lederhofer, J., Acton, O. J., Tsybovsky, Y., Kephart, S. M., Yap, C., Gillespie, R. A., Creanga, A., Olshefsky, A., Stephens, T., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29416-z · Cited by 77
Self-citation
A circular mRNA vaccine prototype producing VFLIP-X spike confers a broad neutralization of SARS-CoV-2 variants by mouse sera
Seephetdee, C., Bhukhai, K., Buasri, N., Leelukkanaveera, P., Lerdwattanasombat, P., Manopwisedjaroen, S., Phueakphud, N., Kuhaudomlarp, S., Olmedillas, E., Saphire, E. O., et al. (2022) · Antiviral Research · doi:10.1016/j.antiviral.2022.105370 · Cited by 73
Broadly neutralizing human antibodies against dengue virus identified by single B cell transcriptomics
Durham, N. D., Agrawal, A., Waltari, E., Croote, D., Zanini, F., Davidson, E., Fouch, M. E., Smith, O., Carabajal, E., Pak, J. E., et al. (2019) · eLife · doi:10.7554/elife.52384 · Cited by 69
The durability of vaccine-induced protection: an overview
Vashishtha, V. M., & Kumar, P. (2024) · Expert Review of Vaccines · doi:10.1080/14760584.2024.2331065 · Cited by 70
Effective high-throughput isolation of fully human antibodies targeting infectious pathogens
Gieselmann, L., Kreer, C., Ercanoglu, M. S., Lehnen, N., Zehner, M., Schommers, P., Potthoff, J., Gruell, H., & Klein, F. (2021) · Nature Protocols · doi:10.1038/s41596-021-00554-w · Cited by 64
Structure of trimeric pre-fusion rabies virus glycoprotein in complex with two protective antibodies
Ng, W. M., Fedosyuk, S., English, S., Augusto, G. S., Berg, A., Thorley, L., Haselon, A.-S., Segireddy, R. R., Bowden, T. A., & Douglas, A. D. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.07.014 · Cited by 64
Safety and Immunogenicity of an mRNA-Based RSV Vaccine Including a 12-Month Booster in a Phase 1 Clinical Trial in Healthy Older Adults
Shaw, C. A., Essink, B. J., Harper, C., Mithani, R., Kapoor, A., Dhar, R., Wilson, L. A., Guo, R., Panozzo, C. A., Wilson, E. M. P., et al. (2024) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiae081 · Cited by 62
A monoclonal antibody against staphylococcal enterotoxin B superantigen inhibits SARS-CoV-2 entry in vitro
Cheng, M. H., Porritt, R. A., Rivas, M. N., Krieger, J., Ozdemir, A. B., Garcia, G., Arumugaswami, V., Fries, B. C., Arditi, M., & Bahar, İ. (2021) · Structure · doi:10.1016/j.str.2021.04.005 · Cited by 59
Mechanisms of antibody-dependent enhancement of infectious disease
Wells, T. J., Esposito, T., Henderson, I. R., & Labzin, L. I. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01067-9 · Cited by 61
Bringing immunofocusing into focus
Musunuri, S., Weidenbacher, P. A. B., & Kim, P. S. (2024) · npj Vaccines · doi:10.1038/s41541-023-00792-x · Cited by 48
Nano-Enabled COVID-19 Vaccines: Meeting the Challenges of Durable Antibody Plus Cellular Immunity and Immune Escape
Nel, A. E., & Miller, J. F. (2021) · ACS Nano · doi:10.1021/acsnano.1c01845 · Cited by 50
Stabilization of the SARS-CoV-2 Spike Receptor-Binding Domain Using Deep Mutational Scanning and Structure-Based Design
Ellis, D., Brunette, N., Crawford, K. H. D., Walls, A. C., Pham, M. N., Chen, C., Herpoldt, K., Fiala, B., Murphy, M., Pettie, D., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.710263 · Cited by 45
Proteome Based Approach Defines Candidates for Designing a Multitope Vaccine against the Nipah Virus
Soltan, M. A., Eldeen, M. A., Elbassiouny, N., Mohamed, I., El-damasy, D. A., Fayad, E., Ali, O. A. A., Raafat, N., Eid, R. A., & Al-Karmalawy, A. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179330 · Cited by 48
Rational Vaccine Design in Times of Emerging Diseases: The Critical Choices of Immunological Correlates of Protection, Vaccine Antigen and Immunomodulation
Schijns, V. E. C. J., Majhen, D., van der Ley, P., Thakur, A., Summerfield, A., Berisio, R., Nativi, C., Fernández‐Tejada, A., Alvarez-Domı́nguez, C., Gizurarson, S. S., et al. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13040501 · Cited by 52
Humoral Immunogenicity of mRNA-1345 RSV Vaccine in Older Adults
Goswami, J., Baqui, A. H., Doreski, P. A., Marc, G. P., Jimenez, G., Ahmed, S., Zaman, K., Duncan, C. J. A., Ujiie, M., Rämet, M., et al. (2024) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiae316 · Cited by 47
Can We AlphaFold Our Way Out of the Next Pandemic?
Higgins, M. K. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167093 · Cited by 48
In Vivo Assembly of Nanoparticles Achieved through Synergy of Structure‐Based Protein Engineering and Synthetic DNA Generates Enhanced Adaptive Immunity
Xu, Z., Wise, M. C., Chokkalingam, N., Walker, S. N., Tello‐Ruiz, E., Elliott, S. T. C., Perales‐Puchalt, A., Xiao, P., Zhu, X., Pumroy, R. A., et al. (2020) · Advanced Science · doi:10.1002/advs.201902802 · Cited by 44
Structure‐guided envelope trimer design in HIV‐1 vaccine development: a narrative review
Derking, R., & Sanders, R. W. (2021) · Journal of the International AIDS Society · doi:10.1002/jia2.25797 · Cited by 46
SARS-CoV-2 Simulations Go Exascale to Capture Spike Opening and Reveal Cryptic Pockets Across the ProteomePreprint
Zimmerman, M. I., Porter, J. R., Ward, M. D., Singh, S., Vithani, N., Meller, A., Mallimadugula, U. L., Kuhn, C. E., Borowsky, J. H., Wiewiora, R., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.27.175430 · Cited by 45
Leveraging deep learning to improve vaccine design
Hederman, A. P., & Ackerman, M. E. (2023) · Trends in Immunology · doi:10.1016/j.it.2023.03.002 · Cited by 41
A Mn 2+ ‐Assisted Nanofiber‐Hydrogel Adjuvant for Simultaneous Enhancement of Humoral and Cellular Immune Responses
Jia, H., Jia, L., Wang, D., Lv, X., Wang, Q., Wang, Z., Liu, J., Yang, L., & Liu, J. (2024) · Advanced Functional Materials · doi:10.1002/adfm.202315442 · Cited by 38
Antigen modifications improve nucleoside-modified mRNA-based influenza virus vaccines in mice
Freyn, A. W., Pine, M., Rosado, V. C., Benz, M., Muramatsu, H., Beattie, M. B., Tam, Y. K., Krammer, F., Palese, P., Nachbagauer, R., et al. (2021) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2021.06.003 · Cited by 37
Potent cross-neutralization of respiratory syncytial virus and human metapneumovirus through a structurally conserved antibody recognition mode
Wen, X., Suryadevara, N., Kose, N., Liu, J., Zhan, X., Handal, L. S., Williamson, L. E., Trivette, A., Carnahan, R. H., Jardetzky, T. S., et al. (2023) · Cell Host & Microbe · doi:10.1016/j.chom.2023.07.002 · Cited by 36
An explainable language model for antibody specificity prediction using curated influenza hemagglutinin antibodies
Wang, Y., Lv, H., Teo, Q. W., Lei, R., Gopal, A. B., Ouyang, W. O., Yeung, Y.-H., Tan, T. J. C., Choi, D., Shen, I. R., et al. (2024) · Immunity · doi:10.1016/j.immuni.2024.07.022 · Cited by 35
Design of a native-like secreted form of the hepatitis C virus E1E2 heterodimer
Guest, J. D., Wang, R., Elkholy, K. H., Chagas, A. C., Chao, K. L., Cleveland, T. E., Kim, Y., Keck, Z., Marin, A., Yunus, A. S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015149118 · Cited by 36
Optimization of a Plasmodium falciparum circumsporozoite protein repeat vaccine using the tobacco mosaic virus platform
Langowski, M. D., Khan, F. A., Bitzer, A. A., Genito, C. J., Schrader, A. J., Martin, M. L., Soto, K., Zou, X., Hadiwidjojo, S., Beck, Z., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911792117 · Cited by 36
Human IgE monoclonal antibody recognition of mite allergen Der p 2 defines structural basis of an epitope for IgE cross-linking and anaphylaxis in vivo
Khatri, K., Richardson, C. M., Glesner, J., Kapingidza, A. B., Mueller, G. A., Zhang, J., Dolamore, C., Vailes, L. D., Wünschmann, S., Peebles, R. S., et al. (2022) · PNAS Nexus · doi:10.1093/pnasnexus/pgac054 · Cited by 34
Safety, Tolerability, and Immunogenicity of an mRNA-Based Respiratory Syncytial Virus Vaccine in Healthy Young Adults in a Phase 1 Clinical Trial
Shaw, C. A., Mithani, R., Kapoor, A., Dhar, R., Wilson, L., Asmar, L. E., Ghamloush, S. S., Schaefers, K., August, A., Stoszek, S., et al. (2024) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiae035 · Cited by 35
An engineered HIV-1 Gag-based VLP displaying high antigen density induces strong antibody-dependent functional immune responses
Tarrés-Freixas, F., Aguilar‐Gurrieri, C., de la Concepción, M. L. R., Urrea, V., Trinité, B., Ortiz, R., Pradenas, E., Blanco, P., Marfil, S., Molinos-Albert, L. M., et al. (2023) · npj Vaccines · doi:10.1038/s41541-023-00648-4 · Cited by 33
Structural Features of Antibody-Peptide Recognition
Lee, J. H., Yin, R. M., Ofek, G., & Pierce, B. G. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.910367 · Cited by 33
Innovations in HIV-1 Vaccine Design
Jones, L. D., Moody, M. A., & Thompson, A. B. (2020) · Clinical Therapeutics · doi:10.1016/j.clinthera.2020.01.009 · Cited by 38
Role of artificial intelligence in peptide vaccine design against RNA viruses
Mohanty, E., & Mohanty, A. (2021) · Informatics in Medicine Unlocked · doi:10.1016/j.imu.2021.100768 · Cited by 34
CircRNA knockdown based on antisense strategies
Aquino‐Jarquín, G. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104066 · Cited by 33
Immune correlates analysis of mRNA-1345 RSV vaccine efficacy clinical trial
Ma, C., Du, J., Lan, L., Kapoor, A., Marc, G. P., Jimenez, G., Duncan, C. J. A., Cam, N. L., Lin, N., Priddy, F. H., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61153-x · Cited by 29
Therapeutic Protein-Based Vaccines
Ahmad, S., Dahiya, V., Vibhuti, A., Pandey, R. P., Tripathi, M. K., & Yadav, M. K. (2023) · Springer eBooks · doi:10.1007/978-981-19-8249-1_13 · Cited by 30
Virus-like Magnetic Mesoporous Silica Particles as a Universal Vaccination Platform against Pathogenic Infections
Liu, M., Zhao, Y. G., Shi, Z., Zink, J. I., & Yu, Q. (2023) · ACS Nano · doi:10.1021/acsnano.3c00644 · Cited by 29
Rational design of uncleaved prefusion-closed trimer vaccines for human respiratory syncytial virus and metapneumovirus
Lee, Y.-Z., Han, J., Zhang, Y.-N., Ward, G., Gomes, K. B., Auclair, S., Stanfield, R. L., He, L., Wilson, I. A., & Zhu, J. (2024) · Nature Communications · doi:10.1038/s41467-024-54287-x · Cited by 33
Cryo-electron tomography of enveloped viruses
Li, S. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.08.005 · Cited by 33
COVID-19, Influenza and RSV: Surveillance-informed prevention and treatment – Meeting report from an isirv-WHO virtual conference
McKimm‐Breschkin, J. L., Hay, A. J., Cao, B., Cox, R. J., Dunning, J. W., Moen, A. C., Olson, D., Pizzorno, A., & Hayden, F. G. (2021) · Antiviral Research · doi:10.1016/j.antiviral.2021.105227 · Cited by 30
Commercial influenza vaccines vary in HA-complex structure and in induction of cross-reactive HA antibodies
Myers, M. L., Gallagher, J. R., Kim, A. J., Payne, W. H., Maldonado-Puga, S., Assimakopoulos, H., Bock, K. W., Torian, U., Moore, I. N., & Harris, A. K. (2023) · Nature Communications · doi:10.1038/s41467-023-37162-z · Cited by 31
Nanovaccines for Advancing Long-Lasting Immunity against Infectious Diseases
Gao, X., Wang, X., Li, S., Rahman, M. S. U., Xu, S., & Liu, Y. (2023) · ACS Nano · doi:10.1021/acsnano.3c07741 · Cited by 27
Protein Oligomer Engineering: A New Frontier for Studying Protein Structure, Function, and Toxicity
Liu, C., & Luo, J. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202216480 · Cited by 25
Recent Advancements in mRNA Vaccines: From Target Selection to Delivery Systems
Wu, Z., Sun, W., & Qi, H. (2024) · Vaccines · doi:10.3390/vaccines12080873 · Cited by 30
A self-assembling nanoparticle: Implications for the development of thermostable vaccine candidates
Liu, Z., Xu, H.-L., Han, G., Tao, L.-N., Lu, Y., Zheng, S., Fang, W., & He, F. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.06.024 · Cited by 25
Longevity of vaccine protection: Immunological mechanism, assessment methods, and improving strategy
Chen, Z., Gao, X., & Yu, D. (2022) · Open Research (University of Surrey) · doi:10.1002/viw.20200103 · Cited by 30
All Eyes on the Prefusion-Stabilized F Construct, but Are We Missing the Potential of Alternative Targets for Respiratory Syncytial Virus Vaccine Design?
Schaerlaekens, S., Jacobs, L., Stobbelaar, K., Cos, P., & Delputte, P. (2024) · Vaccines · doi:10.3390/vaccines12010097 · Cited by 27
AlphaFold2 in biomedical research: facilitating the development of diagnostic strategies for disease
Zhang, H., Lan, J., Wang, H., Lu, R., Zhang, N., He, X., Yang, J., & Chen, L. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1414916 · Cited by 24
Subdominance in Antibody Responses: Implications for Vaccine Development
Lindahl, G. (2020) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00078-20 · Cited by 21
A platform technology for generating subunit vaccines against diverse viral pathogens
Young, A., Isaacs, A., Scott, C. A. P., Modhiran, N., McMillan, C. L. D., Cheung, S. T. M., Barr, J. A., Marsh, G. A., Thakur, N., Bailey, D., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.963023 · Cited by 25
Displaying and delivering viral membrane antigens via WW domain–activated extracellular vesicles
Choi, S., Yang, Z., Wang, Q., Qiao, Z., Sun, M., Wiggins, J., Xiang, S.-H., & Lu, Q. (2023) · Science Advances · doi:10.1126/sciadv.ade2708 · Cited by 24
The broad-spectrum antiviral recommendations for drug discovery against COVID-19
Hazafa, A., ur-Rahman, K., Haq, I. U., Jahan, N., Mumtaz, M., Farman, M. T., Naeem, H., Abbas, F., Naeem, M., Sadiqa, S., et al. (2020) · Drug Metabolism Reviews · doi:10.1080/03602532.2020.1770782 · Cited by 23
Surface-Functionalized Silica-Coated Calcium Phosphate Nanoparticles Efficiently Deliver DNA-Based HIV-1 Trimeric Envelope Vaccines against HIV-1
Li, S., Wang, B., Jiang, S., Pan, Y., Shi, Y., Kong, W., & Shan, Y. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c16989 · Cited by 23
Recombinant protein subunit SARS-CoV-2 vaccines formulated with CoVaccine HT™ adjuvant induce broad, Th1 biased, humoral and cellular immune responses in mice
Lai, C.-Y., To, A., Wong, T. A. S., Lieberman, M. M., Clements, D. E., Senda, J. T., Ball, A. H., Pessaint, L., Andersen, H., Furuyama, W., et al. (2021) · Vaccine X · doi:10.1016/j.jvacx.2021.100126 · Cited by 24
Self-Assembling Nanovaccine Enhances Protective Efficacy Against CSFV in Pigs
Liu, Z., Xu, H.-L., Han, G., Tao, L.-N., Lu, Y., Zheng, S., Fang, W., & He, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.689187 · Cited by 22
Structural and functional analysis of protective antibodies targeting the threefold plateau of enterovirus 71
Huang, K.-Y. A., Zhou, D., Fry, E. E., Kotecha, A., Huang, P.-N., Yang, S.-L., Tsao, K., Huang, Y., Lin, T., Ren, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19013-3 · Cited by 20
Structure-Based and Rational Design of a Hepatitis C Virus Vaccine
Guest, J. D., & Pierce, B. G. (2021) · Viruses · doi:10.3390/v13050837 · Cited by 20
HIV and SARS-CoV-2: Tracing a Path of Vaccine Research and Development
Shepherd, B. L. O., Chang, D., Vasan, S., Ake, J. A., & Modjarrad, K. (2022) · Current HIV/AIDS Reports · doi:10.1007/s11904-021-00597-4 · Cited by 20
Achievement and Challenges in Orthohantavirus Vaccines
Chai, S., Wang, L., Du, H., & Jiang, H. X. (2025) · Vaccines · doi:10.3390/vaccines13020198 · Cited by 19
COVID-19 vaccine design using reverse and structural vaccinology, ontology-based literature mining and machine learning
Huffman, A., Ong, E., Hur, J., D’Mello, A., Tettelin, H., & He, Y. O. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac190 · Cited by 20
Discovery and development of COVID ‐19 vaccine from laboratory to clinic
Saravanan, V., Chagaleti, B. K., Narayanan, P. L., Anandan, V. B., Manoharan, H., Anjana, G. V., Peraman, R., Namasivayam, S. K. R., Kavisri, M., Arockiaraj, J., et al. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14383 · Cited by 19
Structure-Based Design and Antigenic Validation of Respiratory Syncytial Virus G Immunogens
Castrejon, A. M. N., O’Rourke, S. M., Kauvar, L. M., & DuBois, R. M. (2022) · Journal of Virology · doi:10.1128/jvi.02201-21 · Cited by 17
Accelerating clinical trial development in vaccinology: COVID-19 and beyond
Corey, L., & Miner, M. D. (2022) · Current Opinion in Immunology · doi:10.1016/j.coi.2022.102206 · Cited by 17
Historical Advances in Structural and Molecular Biology and How They Impacted Vaccine Development
Koff, W. C., Rappuoli, R., & Plotkin, S. A. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168113 · Cited by 20
Computational formulation of a multiepitope vaccine unveils an exceptional prophylactic candidate against Merkel cell polyomavirus
Imon, R. R., Samad, A., Alam, R., Alsaiari, A. A., Talukder, M. E. K., Almehmadi, M. M., Ahammad, F., & Mohammad, F. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1160260 · Cited by 17
Structure-based design of an immunogenic, conformationally stabilized FimH antigen for a urinary tract infection vaccine
de Monerri, N. C. S., Che, Y., Lees, J. A., Jasti, J., Wu, H., Griffor, M. C., Kodali, S., Hawkins, J. C., Lypowy, J., Ponce, C., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012325 · Cited by 16
How to induce protective humoral immunity against Plasmodium falciparum circumsporozoite protein
Wahl, I., & Wardemann, H. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20201313 · Cited by 17
Efficacy comparison in cap VLPs of PCV2 and PCV3 as swine vaccine vehicle
Qiu, H., Sun, M., Wang, N., Zhang, S., Deng, Z., Xu, H.-L., Yang, H., Gu, H., Fang, W., & He, F. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134955 · Cited by 16
Structural Biology Illuminates Molecular Determinants of Broad Ebolavirus Neutralization by Human Antibodies for Pan-Ebolavirus Therapeutic Development
Murin, C. D., Gilchuk, P., Crowe, J. E., & Ward, A. B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.808047 · Cited by 13
Spike 1 trimer, a nanoparticle vaccine against porcine epidemic diarrhea virus induces protective immunity challenge in piglets
Li, L., Yin, S., Zhou, J., Zhang, L., Teng, Z., Lu, Q., Wang, Y., Yu, J., Zang, H., Ding, Y., et al. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1386136 · Cited by 15
RBD-displaying OMV nanovaccine boosts immunity against SARS-CoV-2
Feng, R., Xue, R., Liu, C., Li, G.-C., Deng, Y., Jin, Z., Liu, J.-Y., Zhang, S., Cheng, H., Guo, M., et al. (2025) · Journal of Nanobiotechnology · doi:10.1186/s12951-025-03191-7 · Cited by 16
Cryo-EM as a powerful tool for drug discovery: recent structural based studies of SARS-CoV-2
Kim, H., & Jung, H. S. (2021) · Han-guk hyeonmigyeong hakoeji/Applied microscopy · doi:10.1186/s42649-021-00062-x · Cited by 14
Immunization with a Prefusion SARS-CoV-2 Spike Protein Vaccine (RBMRNA-176) Protects against Viral Challenge in Mice and Nonhuman Primates
Ma, Q., Li, R., Guo, J., Li, M., Ma, L., Dai, J., Shi, Y., Dai, J., Huang, Y., Dai, C., et al. (2022) · Vaccines · doi:10.3390/vaccines10101698 · Cited by 13

Authors: Graham, B. S., Gilman, M. S. A., & McLellan, J. S.
Affiliations: National Institutes of Health (US)
The University of Texas at Austin (US)
ORCID: Graham, Barney S.
Gilman, Morgan S.A.
McLellan, Jason S.
Venue: Annual Review of Medicine
Publisher: Annual Reviews
Published: 2019-01-27
Volume: 70
Issue: 1
Pages: 91-104
ISSN: 0066-4219 (ISSN-L)
1545-326X
DOI: 10.1146/annurev-med-121217-094234
PMC: PMC6936610
OpenAlex: W2913893387
Cited by: 234
References: 94
Citations by year: 2026: 23 · 2025: 28 · 2024: 40 · 2023: 38 · 2022: 35 · 2021: 41 · 2020: 25 · 2019: 4
FWCI: 2.32
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Annual Review of Medicine (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of Allergy and Infectious Diseases (R01AI127521)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
Keywords: structure-based vaccine design, antigen design, HIV-1 vaccine, respiratory syncytial virus, neutralizing antibodies, monoclonal antibodies, nanoparticle self-assembly, viral surface proteins, class I fusion proteins, emerging pathogens
MeSH terms: Animals, Antibodies, Monoclonal, B-Lymphocytes, Humans, Respiratory Syncytial Viruses, Sensitivity and Specificity, Structure-Activity Relationship, Vaccines, Synthetic, Viral Fusion Proteins, Viral Vaccines, Antibodies, Neutralizing

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Structure-Based Vaccine Antigen Design

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks