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Priyamvada Acharya

Duke University · US
Area of research
Infectious Diseases · Virology
Research interest
Research interests include HIV Research and Treatment, SARS-CoV-2 and COVID-19 Research, Monoclonal and Polyclonal Antibodies Research, and vaccines and immunoinformatics approaches.
h-index
49
citations
10,617
works
217
NIH funding
primary concept
Biology
email

Recent publications

An engineered immunogen activates diverse HIV broadly neutralizing antibody precursors and promotes acquisition of improbable mutations.
2025cited by 5position: contributordoi
Conformational trajectory of the HIV-1 fusion peptide during CD4-induced envelope opening.
2025cited by 4position: contributordoi
Nonstabilized SARS-CoV-2 spike mRNA vaccination induces broadly neutralizing antibodies in nonhuman primates.
2025cited by 1position: contributordoi
An integrated workflow for structural virology with a 100 keV electron microscope
2025cited by 0position: contributordoi
Structural determination of the HIV-1 Variable Region 3 epitope of antibody 19b
2025cited by 0position: contributordoi
Vaccine induction of heterologous HIV-1-neutralizing antibody B cell lineages in humans
Cell 2024cited by 47position: middledoi
SARS-CoV-2 Omicron XBB lineage spike structures, conformations, antigenicity, and receptor recognition.
2024cited by 23position: contributordoi
Conformational flexibility of HIV-1 envelope glycoproteins modulates transmitted/founder sensitivity to broadly neutralizing antibodies.
2024cited by 17position: contributordoi
Microsecond dynamics control the HIV-1 Envelope conformation
Science Advances 2024cited by 16position: middledoi
Microsecond dynamics control the HIV-1 Envelope conformation.
2024cited by 15position: contributordoi
Engineering immunogens that select for specific mutations in HIV broadly neutralizing antibodies
Nature Communications 2024cited by 12position: contributordoi
Structural Studies of Henipavirus Glycoproteins.
2024cited by 11position: contributordoi
SARS-CoV-2 Omicron XBB lineage spike structures, conformations, antigenicity, and receptor recognition
2024cited by 2position: contributordoi
Conformational trajectory of the HIV-1 fusion peptide during CD4-induced envelope opening
2024cited by 0position: contributordoi
Evolution of the SARS-CoV-2 Omicron spike.
2023cited by 64position: contributordoi
Structural basis for breadth development in the HIV-1 V3-glycan targeting DH270 antibody clonal lineage.
2023cited by 19position: contributordoi
Vaccine Induction of Heterologous HIV-1 Neutralizing Antibody B Cell Lineages in Humans
medRxiv 2023cited by 7position: middledoi
Structures of Langya virus fusion protein ectodomain in pre and post fusion conformation
2023cited by 0position: contributordoi
Structural diversity of the SARS-CoV-2 Omicron spike.
2022cited by 195position: contributordoi
A broadly cross-reactive antibody neutralizes and protects against sarbecovirus challenge in mice.
2022cited by 117position: contributordoi
Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike.
2022cited by 103position: contributordoi
Stabilized HIV-1 envelope immunization induces neutralizing antibodies to the CD4bs and protects macaques against mucosal infection.
2022cited by 35position: contributordoi
Transient transfection and purification of SARS-CoV-2 spike protein from mammalian cells.
2022cited by 7position: contributordoi
Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike
2022cited by 2position: contributordoi
Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity.
2021cited by 346position: contributordoi
In vitro and in vivo functions of SARS-CoV-2 infection-enhancing and neutralizing antibodies
Cell 2021cited by 331position: middledoi
D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization.
2021cited by 302position: contributordoi
D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction.
2021cited by 285position: contributordoi
Neutralizing antibody vaccine for pandemic and pre-emergent coronaviruses.
2021cited by 250position: contributordoi
Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies.
2021cited by 88position: contributordoi

Grants

No grants ingested yet.

Frequent collaborators

· 27 papers (2020–2025)Robert J. Edwards · United States Army Medical Research Institute of Infectious Diseases17 papers (2019–2025) · 13 papers (2020–2025)Kevin O. Saunders · Integrative Medicine Institute9 papers (2019–2025)Barton F. Haynes · Duke University School of Medicine8 papers (2020–2025) · 8 papers (2020–2024)Peter D. Kwong · National Institutes of Health7 papers (2013–2025) · 6 papers (2021–2025)Gregory D. Sempowski · RTI International5 papers (2020–2022) · 5 papers (2019–2024)Mario J. Borgnia · Duke University4 papers (2019–2020) · 4 papers (2021–2024)Bette Korber · Los Alamos Medical Center3 papers (2021–2024)Robert Parks · International Vaccine Institute3 papers (2020–2025) · 3 papers (2021–2024) · 3 papers (2021–2021)Allen L. Hsu · Columbia University3 papers (2019–2020)Scott C. Blanchard · St. Jude Children's Research Hospital2 papers (2020–2020)S. Munir Alam · Duke University2 papers (2020–2024)Rory Henderson · Duke University2 papers (2020–2024)