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Ema T. Crooks
Researcher at Torrey Pines Institute for Molecular Studies
Publications - 15
Citations - 1279
Ema T. Crooks is an academic researcher from Torrey Pines Institute for Molecular Studies. The author has contributed to research in topics: Neutralizing antibody & Epitope. The author has an hindex of 11, co-authored 15 publications receiving 1135 citations.
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Journal ArticleDOI
Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies.
Nicole A. Doria-Rose,Chaim A. Schramm,Jason Gorman,Penny L. Moore,Jinal N. Bhiman,Brandon J. DeKosky,Michael J. Ernandes,Ivelin S. Georgiev,Helen J. Kim,Marie Pancera,Ryan P. Staupe,Han Altae-Tran,Robert T. Bailer,Ema T. Crooks,Albert Cupo,Aliaksandr Druz,Nigel Garrett,Kam Hon Hoi,Rui Kong,Mark K. Louder,Nancy S. Longo,Krisha McKee,Molati Nonyane,Sijy O'Dell,Ryan S. Roark,Rebecca S. Rudicell,Stephen D. Schmidt,Daniel J. Sheward,Cinque Soto,Constantinos Kurt Wibmer,Yongping Yang,Zhenhai Zhang,Nisc Comparative Sequencing,James C. Mullikin,James M. Binley,Rogier W. Sanders,Ian A. Wilson,John P. Moore,Andrew B. Ward,George Georgiou,Carolyn Williamson,Salim S. Abdool Karim,Lynn Morris,Peter D. Kwong,Lawrence Shapiro,John R. Mascola +45 more
TL;DR: HIV-1 V1V2-directed neutralizing antibodies can develop relatively rapidly through initial selection of B cells with a long CDR H3, and limited subsequent somatic hypermutation, and provide important insights relevant to HIV-1 vaccine development.
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Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site
Ema T. Crooks,Tommy Tong,Bimal K. Chakrabarti,Kristin Narayan,Ivelin S. Georgiev,Sergey Menis,Sergey Menis,Xiaoxing Huang,Daniel W. Kulp,Daniel W. Kulp,Keiko Osawa,Janelle Muranaka,Guillaume Stewart-Jones,Guillaume Stewart-Jones,Joanne DeStefano,Sijy O'Dell,Celia C. LaBranche,James E. Robinson,David C. Montefiori,Krisha McKee,Sean X. Du,Nicole A. Doria-Rose,Peter D. Kwong,John R. Mascola,Ping Zhu,William R. Schief,William R. Schief,William R. Schief,Richard T. Wyatt,Richard T. Wyatt,Robert G. Whalen,James M. Binley +31 more
TL;DR: The data show for the first time that strain-specific holes in the glycan fence can allow the development of tier 2 neutralizing antibodies to native spikes, and cross-neutralization can occur in the absence of protecting glycan.
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Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected.
TL;DR: Remarkably, sequential glycosidase-protease digests led to a complete or near-complete removal of junk Env from many viral strains, leaving trimers and viral infectivity largely intact.
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HIV-1 Virus-Like Particles Bearing Pure Env Trimers Expose Neutralizing Epitopes but Occlude Nonneutralizing Epitopes
TL;DR: It is shown that nonfunctional Env can be selectively cleared from virus-like particle (VLP) surfaces by enzyme digests, and a scatterplot analysis revealed a strong correlation between MAb binding and neutralization of trimer VLPs, suggesting that trimerVLPs bear essentially pure native trimer that should allow its unfettered evaluation in a vaccine setting.
Journal ArticleDOI
Virus-like Particles Identify an HIV V1V2 Apex-Binding Neutralizing Antibody that Lacks a Protruding Loop
Evan M. Cale,Jason Gorman,Nathan Radakovich,Ema T. Crooks,Keiko Osawa,Tommy Tong,Jiaqi Li,R. Nagarajan,Gabriel Ozorowski,David R. Ambrozak,Mangai Asokan,Robert T. Bailer,Anthony K. Bennici,Xuejun Chen,Nicole A. Doria-Rose,Aliaksandr Druz,Yu Feng,M. Gordon Joyce,Mark K. Louder,Sijy O'Dell,Courtney Oliver,Marie Pancera,Mark Connors,Thomas J. Hope,Thomas B. Kepler,Richard T. Wyatt,Andrew B. Ward,Ivelin S. Georgiev,Peter D. Kwong,John R. Mascola,James M. Binley +30 more
TL;DR: A lineage of HIV‐1‐neutralizing antibodies that target the envelope trimer apex is isolated by using virus‐like particles and conformationally stabilized Env trimers as B cell probes and reveals a binding mode involving side‐chain‐to‐side‐chain interactions that reduced the distance the antibody loop must traverse the glycan shield, thereby facilitating V1V2 binding via a non‐protruding loop.