A. B. Ward

This paper develops a therapeutic cocktail of two human antibodies that protect against multiple ebolaviruses in non-human primates and reveals their molecular mechanisms.

This paper uses cryoEM and next-generation sequencing to identify monoclonal antibodies from polyclonal sera and validate their antigen-binding properties.

This study shows that immunization with a thermostable HIV-1 clade C Env trimer induces potent autologous neutralizing antibodies in rabbits, with distinct epitope specificity compared to natural infection.

This study evaluates murine monoclonal antibodies against SARS-CoV-2 RBD, showing neutralization of wild-type and variants, and in vivo protection dependent on neutralization.

This study identifies ultrapotent bispecific antibodies that neutralize emerging SARS-CoV-2 variants by targeting multiple spike protein regions, showing efficacy in vitro and in a hamster model.

This study identifies a class of broadly neutralizing antibodies targeting a conserved membrane-proximal epitope on influenza HA, showing their induction by a chimeric HA vaccine.

This study shows that off-target antibodies from HIV trimer vaccines cause trimer disassembly, exposing more off-target epitopes and driving further off-target immune responses.

The paper examines how mutations at E484 and K417 in SARS-CoV-2 variants affect neutralizing antibodies, showing reduced efficacy against certain antibody families but not others.

This study shows that combining cross-neutralizing antibodies CV38-142 and COVA1-16 enhances neutralization of SARS-CoV-2 and SARS-CoV pseudoviruses.

The paper uses cryoEM to analyze polyclonal antibody responses to HIV Env immunogens in rhesus macaques, revealing structural differences in antibody binding and immunogenicity of engineered mutations and glycan sites.

The paper identifies common genetic and structural features of human antibodies recognizing the influenza HA trimer interface, suggesting it as a target for vaccine design.

This study isolates HIV-1 neutralizing antibodies from mice and rabbits immunized with gp41-stabilized trimers and nanoparticles, showing they target different epitopes and elicit Env-dependent breadth.

This study shows SARS-CoV-2 spike protein binds to heparan sulfate and ACE2 on cells codependently, forming a complex that facilitates infection, suggesting potential therapeutic targets.

This study uses cryo-EM, computational modeling, and mass-spectrometry to analyze the HIV-1 Env glycan shield's structure and dynamics, revealing how heterogeneity and interactions affect epitope accessibility and trimer stability.

This study maps the neutralizing and binding specificities of polyclonal rabbit serum against HIV Env trimers using mutational antigenic profiling and EMPEM.

The paper presents cryo-EM structures of glycan cap antibodies that neutralize ebolavirus by targeting a conserved MLD-anchor site, revealing common features among broadly neutralizing antibodies.

The paper examines cross-reactive serum and memory B cell responses to SARS-CoV-2 and endemic coronaviruses, finding weak serum cross-reactivity but stronger memory B cell cross-reactivity.

This study identifies a single amino acid mutation that determines the difference in neutralization ability of a cross-reactive antibody between SARS-CoV-2 and SARS-CoV.

This study designs and tests Ebola virus vaccines using stabilized GP trimers displayed on nanoparticles, showing they induce neutralizing antibodies and enhance infection.

The paper uses cryo-EM and glycan analysis to study the structure of a full-length SARS-CoV-2 spike protein in a vaccine candidate, revealing its stable prefusion conformation and novel trimer interactions.

The paper identifies a SARS-CoV-2 antibody that cross-neutralizes SARS-CoV by binding a conserved epitope and relies on avidity for neutralization.

This study identifies an alternative binding mode of IGHV3-53 antibodies to the SARS-CoV-2 RBD, showing that longer CDR H3 can bind with different angles and interactions.

The paper identifies a strain-specific HIV-1 inhibitor targeting a pocket near the fusion peptide, demonstrating small molecules can disrupt viral fusion and offering a template for drug design.

The paper quantifies the resilience and vulnerability of HIV-1's glycan shield using atomistic modeling and graph theory, revealing new insights into its structure and potential for immunogen design.

The paper investigates how HIV-1 envelope glycan networks affect the formation and stability of broadly neutralizing antibody epitopes, showing their importance in immunogen design.

This study identifies vulnerabilities in coronavirus glycan shields by showing that MERS S protein has under-processed oligomannose-type glycan clusters, unlike SARS and HKU1 CoVs, and that these glycans do not form an effective shield against antibodies.

This study maps antibody responses to HIV-1 envelope trimers in non-human primates, identifying strain-specific and conserved epitopes recognized by vaccine-induced antibodies.

The paper evaluates de novo-designed two-component nanoparticles for presenting HIV Env trimers, showing improved antibody responses through multivalent display.