Andrew B Ward


Affiliation: The Scripps Research Institute
Country: USA


  1. Ozorowski G, Cupo A, Golabek M, LoPiccolo M, Ketas T, Cavallary M, et al. Effects of Adjuvants on HIV-1 Envelope Glycoprotein SOSIP Trimers In Vitro. J Virol. 2018;92: pubmed publisher
  2. Crispin M, Ward A, Wilson I. Structure and Immune Recognition of the HIV Glycan Shield. Annu Rev Biophys. 2018;: pubmed publisher
    ..Please see for revised estimates. ..
  3. Ward A. Playing Chess with HIV. Immunity. 2019;50:283-285 pubmed publisher
    ..Dingens et al. (2019) use saturating mutagenesis of Env to play out all of the potential bnAb escape strategies and in doing so define the functional epitopes of these important vaccine and immunotherapeutic targets. ..
  4. Murin C, Wilson I, Ward A. Antibody responses to viral infections: a structural perspective across three different enveloped viruses. Nat Microbiol. 2019;4:734-747 pubmed publisher
  5. Wu N, Ward A. Deception through Mimicry: A Cellular Antiviral Strategy. Cell. 2018;175:1728-1729 pubmed publisher
    ..identify a novel antiviral restriction factor, RBBP6, by characterizing the cellular interactome of Ebola virus. RBBP6 targets the Ebola virus transcription factor VP30 by mimicking the binding of Ebola virus nucleoprotein. ..
  6. Kirchdoerfer R, Wang N, Pallesen J, Wrapp D, Turner H, Cottrell C, et al. Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis. Sci Rep. 2018;8:15701 pubmed publisher
    ..Neither binding to ACE2 nor cleavage by trypsin at the S1/S2 cleavage site impart large conformational changes within stabilized SARS-CoV S or expose the secondary cleavage site, S2'. ..
  7. Murin C, Bruhn J, Bornholdt Z, Copps J, Stanfield R, Ward A. Structural Basis of Pan-Ebolavirus Neutralization by an Antibody Targeting the Glycoprotein Fusion Loop. Cell Rep. 2018;24:2723-2732.e4 pubmed publisher
    ..Our structures provide a more complete description of the ebolavirus immunogenic landscape, as well as a molecular basis for how rare but potent antibodies target conserved filoviral fusion machinery. ..
  8. Bianchi M, Turner H, Nogal B, Cottrell C, Oyen D, Pauthner M, et al. Electron-Microscopy-Based Epitope Mapping Defines Specificities of Polyclonal Antibodies Elicited during HIV-1 BG505 Envelope Trimer Immunization. Immunity. 2018;49:288-300.e8 pubmed publisher
    ..Our method provides an efficient and semiquantitative map of epitopes that are targeted in a polyclonal antibody response and should be of widespread utility in vaccine and infection studies. ..
  9. Rantalainen K, Berndsen Z, Murrell S, Cao L, Omorodion O, Torres J, et al. Co-evolution of HIV Envelope and Apex-Targeting Neutralizing Antibody Lineage Provides Benchmarks for Vaccine Design. Cell Rep. 2018;23:3249-3261 pubmed publisher
    ..These studies therefore provide important guideposts for design of immunogens that prime and mature nAb responses to the Env V2-apex. ..

More Information


  1. Lee J, Andrabi R, Su C, Yasmeen A, Julien J, Kong L, et al. A Broadly Neutralizing Antibody Targets the Dynamic HIV Envelope Trimer Apex via a Long, Rigidified, and Anionic ?-Hairpin Structure. Immunity. 2017;46:690-702 pubmed publisher
    ..Overall, the findings exemplify the creative solutions that the human immune system can evolve to recognize a conserved motif buried under a canopy of glycans. ..
  2. Nogal B, Bowman C, Ward A. Time-course, negative-stain electron microscopy-based analysis for investigating protein-protein interactions at the single-molecule level. J Biol Chem. 2017;292:19400-19410 pubmed publisher
    ..Moreover, our method provides critical insights into broadly neutralizing antibody recognition of Env, which may inform vaccine immunogen design and immunotherapeutic development. ..