E
Erica Ollmann Saphire
Researcher at La Jolla Institute for Allergy and Immunology
Publications - 208
Citations - 20187
Erica Ollmann Saphire is an academic researcher from La Jolla Institute for Allergy and Immunology. The author has contributed to research in topics: Ebola virus & Antibody. The author has an hindex of 54, co-authored 169 publications receiving 14463 citations. Previous affiliations of Erica Ollmann Saphire include Scripps Health & University of California, San Diego.
Papers
More filters
Journal ArticleDOI
Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus.
Bette T. Korber,Will Fischer,Sandrasegaram Gnanakaran,Hyejin Yoon,James Theiler,Werner Abfalterer,Nick Hengartner,Elena E. Giorgi,Tanmoy Bhattacharya,Brian T. Foley,Kathryn M. Hastie,Matthew Parker,David G Partridge,Cariad Evans,Timothy M. Freeman,Thushan I de Silva,Adrienne Angyal,Rebecca Brown,Laura Carrilero,Luke R. Green,Luke R. Green,Luke R. Green,Danielle C. Groves,Katie Johnson,Alexander J Keeley,Benjamin B Lindsey,Paul J. Parsons,Mohammad Raza,Sarah Rowland-Jones,Nikki Smith,Rachel Tucker,Dennis Wang,Matthew Wyles,Charlene McDanal,Lautaro G. Perez,Haili Tang,Alex Moon-Walker,Alex Moon-Walker,Alex Moon-Walker,Sean P. J. Whelan,Celia C. LaBranche,Erica Ollmann Saphire,David C. Montefiori +42 more
TL;DR: A SARS-CoV-2 variant carrying the Spike protein amino acid change D614G has become the most prevalent form in the global pandemic, and it is found that the G614 variant grows to higher titer as pseudotyped virions.
Journal ArticleDOI
Immunological memory to SARS-CoV-2 assessed for up to 8 months after infection.
Jennifer M. Dan,Jennifer M. Dan,Jose Mateus,Yu Kato,Kathryn M. Hastie,Esther Dawen Yu,Caterina E. Faliti,Alba Grifoni,Sydney I. Ramirez,Sydney I. Ramirez,Sonya Haupt,April Frazier,Catherine Nakao,Vamseedhar Rayaprolu,Stephen A. Rawlings,Bjoern Peters,Bjoern Peters,Florian Krammer,Viviana Simon,Erica Ollmann Saphire,Erica Ollmann Saphire,Davey M. Smith,Daniela Weiskopf,Alessandro Sette,Alessandro Sette,Shane Crotty,Shane Crotty +26 more
TL;DR: This article analyzed multiple compartments of circulating immune memory to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in 254 samples from 188 COVID-19 cases, including 43 samples at ≥ 6 months after infection.
Journal ArticleDOI
Antigen-Specific Adaptive Immunity to SARS-CoV-2 in Acute COVID-19 and Associations with Age and Disease Severity.
Carolyn Rydyznski Moderbacher,Sydney I. Ramirez,Sydney I. Ramirez,Jennifer M. Dan,Jennifer M. Dan,Alba Grifoni,Kathryn M. Hastie,Daniela Weiskopf,Simon Bélanger,Robert K. Abbott,Christina K. Kim,Jinyong Choi,Yu Kato,Eleanor G. Crotty,Cheryl Kim,Stephen A. Rawlings,Jose Mateus,Longping V. Tse,April Frazier,Ralph S. Baric,Bjoern Peters,Jason A. Greenbaum,Erica Ollmann Saphire,Erica Ollmann Saphire,Davey M. Smith,Alessandro Sette,Alessandro Sette,Shane Crotty,Shane Crotty +28 more
TL;DR: A combined examination of all three branches of adaptive immunity at the level of SARS-CoV-2-specific CD4+ and CD8+ T cell and neutralizing antibody responses in acute and convalescent subjects suggested roles for both CD4 plus T cells in protective immunity in COVID-19.
Journal ArticleDOI
Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design.
Erica Ollmann Saphire,Paul W. H. I. Parren,Ralph Pantophlet,Michael B. Zwick,Garrett M. Morris,Pauline M. Rudd,Raymond A. Dwek,Robyn L. Stanfield,Dennis R. Burton,Ian A. Wilson +9 more
TL;DR: The crystal structure at 2.7 angstrom resolution of the human antibody IgG1 b12 provides a rationale for the extensive cross-reactivity of b12 and a valuable framework for the design of HIV-1 vaccines capable of eliciting b12-like activity.
Journal ArticleDOI
Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41.
Michael B. Zwick,Aran F. Labrijn,Min Wang,Catherine Spenlehauer,Erica Ollmann Saphire,James M. Binley,John P. Moore,Gabriela Stiegler,Hermann Katinger,Dennis R. Burton,Paul W. H. I. Parren +10 more
TL;DR: The results suggest that a rather extensive region of gp41 close to the transmembrane domain is accessible to neutralizing Abs and could form a useful target for vaccine design.