The People of Tulane Cancer Center Research
His work employs biochemical and biophysical techniques, including nuclear magnetic resonance (NMR) spectroscopy to investigate structure/function relationships in protein-protein interactions, especially those involved in cellular stress and immune responses. Molecular chaperones are implicated in a variety of cellular processes, including DNA replication, gene expression, and protein translocation across membranes, in addition to the heat shock response. The goal of this research is to understand at a physical chemical level how Escherichia coli molecular chaperones cooperate in the management of protein-protein interactions. Dr. Landry's research has included study of the structural instability and T-cell epitope immunodominance. Humoral and cellular immunity to HIV and other pathogens depend on antigen-specific CD4+ T cell responses directed against peptides presented in MHC class II antigen presenting proteins. Generally, CD4+ T-cell responses are focused on only a few immunodominant regions of naturally processed antigens. We have found that immunodominant regions occur in the sequences flanking locally unstable segments of an antigen's three-dimensional structure, and we are now modifying CD4+ helper T-cell immune responses to recombinant antigens by engineering their processing and presentation.
Mirano-Bascos D, Tary-Lehmann M and Landry SJ, Antigen structure influences helper T-cell epitope dominance in the human immune response to HIV envelope glycoprotein gp120, European Journal of Immunology 2008; 38:1-7.
Melton SJ and Landry SJ, Three dimensional structure directs T-cell epitope dominance associated with allergy, Clinical and Molecular Allergy, 2008; 6:9.
Li H, Xu C-F, Blais S, Wan Q, Zhang H-T, Kong X, Landry SJ and Hioe CE, Proximal glycans outside of the epitopes regulate the presentation of HIV-1 envelope gp120 helper epitopes, Journal of Immunology, 2009; 182:6369-6378.
Mirano-Bascos D, Steede NK, Robinson JE and Landry SJ, Influence of disulfide-stabilized structure on the specificity of helper T-cell and antibody responses to HIV envelope glycoprotein gp120, Journal of Virology 2010; 84:3303-3311.
Curiel TJ, Morris C, Brumlik M, Landry SJ, Finstad K, Nelson A, Joshi V, Hawkins C, Alarez X, Lackner A, Mohamadzadeh M, Peptides identified through phage display direct immunogenic antigen to dendritic cells, The Journal of Immunology 2004;172:7425-7431.
Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ, A mobile loop order-disorder transition modulates the speed of chaperonin cycling, Protein Science 2004;13:2139-2148.
Carmicle S, Steede NK and Landry SJ, Antigen three-dimensional structure guides the processing and presentation of helper T-cell epitopes, Molecular Immunology 2006; 44:1159-1168.
Horne BE, Li T, Genevaux P, Georgopoulos C and Landry SJ, The hsp40 J-domain stimulates hsp70 when tethered by the client to the ATPase domain, Journal of Biological Chemistry, accepted for publication.
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