Ashliegh Williams

ORCID: 0009-0009-9212-6834
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About
Contact & Profiles
Research Areas
  • HIV Research and Treatment
  • Protein Structure and Dynamics
  • Transgenic Plants and Applications
  • RNA and protein synthesis mechanisms
  • HIV/AIDS drug development and treatment
  • Monoclonal and Polyclonal Antibodies Research
  • vaccines and immunoinformatics approaches
  • Bacteriophages and microbial interactions

Duke Medical Center
2023-2024

Duke University
2023

The HIV-1 Envelope (Env) glycoprotein facilitates host cell fusion through a complex series of receptor-induced structural changes. Although remarkable progress has been made in understanding the structures various Env conformations, microsecond timescale dynamics have not studied experimentally. Here, we used time-resolved, temperature-jump small-angle x-ray scattering to monitor rearrangements an SOSIP ectodomain construct with precision. In two distinct variants, detected transition that...

10.1126/sciadv.adj0396 article EN cc-by-nc Science Advances 2024-02-02

Vaccine development targeting rapidly evolving pathogens such as HIV-1 requires induction of broadly neutralizing antibodies (bnAbs) with conserved paratopes and mutations, in some cases, the same Ig-heavy chains. The current trial-and-error search for immunogen modifications that improve selection specific bnAb mutations is imprecise. Here, to precisely engineer boosting immunogens, we use molecular dynamics simulations examine encounter states form when collide Envelope (Env). By mapping...

10.1038/s41467-024-53120-9 article EN cc-by-nc-nd Nature Communications 2024-11-03

Abstract Vaccine development targeting rapidly evolving pathogens such as HIV-1 requires induction of broadly neutralizing antibodies (bnAbs) with conserved paratopes and mutations, and, in some cases, the same Ig-heavy chains. The current trial-and-error search for immunogen modifications that improve selection specific bnAb mutations is imprecise. To precisely engineer boosting immunogens, we used molecular dynamics simulations to examine encounter states form when collide Envelope (Env)....

10.1101/2023.12.15.571700 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-12-16

Abstract The HIV-1 Envelope (Env) glycoprotein facilitates host cell fusion through a complex series of receptor-induced structural changes. Although significant progress has been made in understanding the structures various Env conformations and transition intermediates that occur within millisecond timescale, faster transitions microsecond timescale have not yet observed. In this study, we employed time-resolved, temperature-jump small angle X- ray scattering to monitor rearrangements an...

10.1101/2023.05.17.541130 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2023-05-18
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