C
Cinque Soto
Researcher at Vanderbilt University Medical Center
Publications - 59
Citations - 8071
Cinque Soto is an academic researcher from Vanderbilt University Medical Center. The author has contributed to research in topics: Epitope & Antibody. The author has an hindex of 32, co-authored 56 publications receiving 6994 citations. Previous affiliations of Cinque Soto include University of Pennsylvania & Vaccine Research Center.
Papers
More filters
Journal ArticleDOI
Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus
Jason S. McLellan,Man Chen,M. Gordon Joyce,Mallika Sastry,Guillaume Stewart-Jones,Yongping Yang,Baoshan Zhang,Lei Chen,Sanjay Srivatsan,Anqi Zheng,Tongqing Zhou,Kevin W. Graepel,Azad Kumar,Syed M. Moin,Jeffrey C. Boyington,Gwo-Yu Chuang,Cinque Soto,Ulrich Baxa,Arjen Q. Bakker,Hergen Spits,Tim Beaumont,Zizheng Zheng,Ningshao Xia,Sung Youl Ko,John Paul Todd,Srinivas S. Rao,Barney S. Graham,Peter D. Kwong +27 more
TL;DR: A viral antigen is sought that provides greater protection than currently available vaccines and focused on antigenic site Ø, a metastable site specific to the prefusion state of the RSV fusion (F) glycoprotein, as this site is targeted by extremely potent RSV-neutralizing antibodies.
Journal ArticleDOI
Structure and immune recognition of trimeric pre-fusion HIV-1 Env
Marie Pancera,Tongqing Zhou,Aliaksandr Druz,Ivelin S. Georgiev,Cinque Soto,Jason Gorman,Jinghe Huang,Priyamvada Acharya,Gwo-Yu Chuang,Gilad Ofek,Guillaume Stewart-Jones,Jonathan Stuckey,Robert T. Bailer,M. Gordon Joyce,Mark K. Louder,Nancy Tumba,Yongping Yang,Baoshan Zhang,Myron S. Cohen,Barton F. Haynes,John R. Mascola,Lynn Morris,James B. Munro,Scott C. Blanchard,Walther Mothes,Mark Connors,Peter D. Kwong +26 more
TL;DR: The structure at 3.5 Å resolution for an HIV-1 Env trimer captured in a mature closed state by antibodies PGT122 and 35O22 is reported, revealing the pre-fusion conformation of gp41, rearrangements needed for fusion activation, and defines parameters of immune evasion and immune recognition.
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.
Journal ArticleDOI
Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers
TL;DR: Solid-state NMR spectroscopy indicates that amantadine physically occludes the M2 channel, thus paving the way for developing new antiviral drugs against influenza viruses and demonstrates the ability of solid- state NMR to elucidate small-molecule interactions with membrane proteins and determine high-resolution structures of their complexes.
Journal ArticleDOI
Structural basis for the function and inhibition of an influenza virus proton channel
Amanda L. Stouffer,Amanda L. Stouffer,Rudresh Acharya,David Salom,Anna S. Levine,Luigi Di Costanzo,Cinque Soto,Valentina Tereshko,Vikas Nanda,Steven Stayrook,William F. DeGrado +10 more
TL;DR: The crystal structure of the transmembrane-spanning region of the homotetrameric protein in the presence and absence of the channel-blocking drug amantadine provides a starting point for solving the problem of resistance to M2-channel blockers.