Jason S McLellan

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. pmc Structure of a major antigenic site on the respiratory syncytial virus fusion glycoprotein in complex with neutralizing antibody 101F
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Virol 84:12236-44. 2010
  2. pmc Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virus
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    J Mol Biol 409:853-66. 2011
  3. pmc Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes
    Jason S McLellan
    Vaccine Research Center, NIAID NIH, 40 Convent Drive, Bldg 40, Rm 2613B, Bethesda, MD 20892, USA
    J Virol 85:7788-96. 2011
  4. doi request reprint Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16
    Marie Pancera
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, US National Institutes of Health, Bethesda, Maryland, USA
    Nat Struct Mol Biol 20:804-13. 2013
  5. pmc Structural basis for norovirus inhibition and fucose mimicry by citrate
    Grant S Hansman
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Virol 86:284-92. 2012
  6. pmc N332-Directed broadly neutralizing antibodies use diverse modes of HIV-1 recognition: inferences from heavy-light chain complementation of function
    Marie Pancera
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America
    PLoS ONE 8:e55701. 2013
  7. doi request reprint Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 340:1113-7. 2013
  8. pmc Structural basis of respiratory syncytial virus neutralization by motavizumab
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    Nat Struct Mol Biol 17:248-50. 2010
  9. doi request reprint Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 342:592-8. 2013
  10. pmc A short segment of the HIV-1 gp120 V1/V2 region is a major determinant of resistance to V1/V2 neutralizing antibodies
    Nicole A Doria-Rose
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    J Virol 86:8319-23. 2012

Collaborators

Detail Information

Publications14

  1. pmc Structure of a major antigenic site on the respiratory syncytial virus fusion glycoprotein in complex with neutralizing antibody 101F
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Virol 84:12236-44. 2010
    ..Collectively, these results provide a structural basis for RSV neutralization by antibodies that target a major antigenic site on the fusion glycoprotein...
  2. pmc Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virus
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    J Mol Biol 409:853-66. 2011
    ....
  3. pmc Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes
    Jason S McLellan
    Vaccine Research Center, NIAID NIH, 40 Convent Drive, Bldg 40, Rm 2613B, Bethesda, MD 20892, USA
    J Virol 85:7788-96. 2011
    ..The structural preservation of neutralizing epitopes in the postfusion state suggests that this conformation can elicit neutralizing antibodies and serve as a useful vaccine antigen...
  4. doi request reprint Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16
    Marie Pancera
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, US National Institutes of Health, Bethesda, Maryland, USA
    Nat Struct Mol Biol 20:804-13. 2013
    ..Although HIV-1-glycan diversity facilitates evasion, antibody somatic diversity can overcome this and can provide clues to guide the design of modified antibodies with enhanced neutralization. ..
  5. pmc Structural basis for norovirus inhibition and fucose mimicry by citrate
    Grant S Hansman
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Virol 86:284-92. 2012
    ..Importantly, competition STD NMR showed that citrate could compete with HBGA for norovirus binding. Together, the results suggest that citrate and other glycomimetics have the potential to block human noroviruses from binding to HBGAs...
  6. pmc N332-Directed broadly neutralizing antibodies use diverse modes of HIV-1 recognition: inferences from heavy-light chain complementation of function
    Marie Pancera
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America
    PLoS ONE 8:e55701. 2013
    ..Overall, our results add to the growing body of evidence that the human immune system is capable of recognizing the N332-region of HIV-1 gp120 in diverse ways...
  7. doi request reprint Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 340:1113-7. 2013
    ..These studies should enable design of improved vaccine antigens and define new targets for passive prevention of RSV-induced disease...
  8. pmc Structural basis of respiratory syncytial virus neutralization by motavizumab
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    Nat Struct Mol Biol 17:248-50. 2010
    ..Modeling suggests that motavizumab recognizes a different quaternary configuration of the F glycoprotein than that observed in a homologous structure...
  9. doi request reprint Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 342:592-8. 2013
    ..Immunization with site Ø-stabilized variants of RSV F in mice and macaques elicited levels of RSV-specific neutralizing activity many times the protective threshold. ..
  10. pmc A short segment of the HIV-1 gp120 V1/V2 region is a major determinant of resistance to V1/V2 neutralizing antibodies
    Nicole A Doria-Rose
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    J Virol 86:8319-23. 2012
    ....
  11. pmc Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nature 480:336-43. 2011
    ..In addition to structurally defining V1/V2, the results thus identify a paradigm of antibody recognition for highly glycosylated antigens, which-with PG9-involves a site of vulnerability comprising just two glycans and a strand...
  12. pmc Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-SIGN to activate ERK1 and ERK2
    Teresa R Johnson
    Viral Pathogenesis Laboratorya and Structural Biology Section, b Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    J Virol 86:1339-47. 2012
    ....
  13. pmc Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1
    Marie Pancera
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892 3027, USA
    J Virol 84:8098-110. 2010
    ..The structural and functional details of extraordinary CDR H3 and extensive affinity maturation provide insights into the neutralization mechanism of and the elicitation pathway for broadly neutralizing antibodies like PG9 and PG16...
  14. pmc Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability
    Grant S Hansman
    Structural Biology Section, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, 40 Convent Drive, Building 40, Room 4508, National Institutes of Health, Bethesda, MD 20892, USA
    J Virol 85:6687-701. 2011
    ..Despite this evasion tactic, the HBGA site of viral vulnerability may provide a viable target for small molecule- and antibody-mediated neutralization of GII norovirus...