Pick Topic
Review Topic
List Experts
Examine Expert
Save Expert
  Site Guide ··   
Melanoma: HELP
Articles by Brian M. Baker
Based on 6 articles published since 2010
(Why 6 articles?)
||||

Between 2010 and 2020, Brian M. Baker wrote the following 6 articles about Melanoma.
 
+ Citations + Abstracts
1 Article Molecular properties of gp100-reactive T-cell receptors drive the cytokine profile and antitumor efficacy of transgenic host T cells. 2019

Eby, Jonathan M / Smith, Angela R / Riley, Timothy P / Cosgrove, Cormac / Ankney, Christian M / Henning, Steven W / Paulos, Chrystal M / Garrett-Mayer, Elizabeth / Luiten, Rosalie M / Nishimura, Michael I / Baker, Brian M / Le Poole, I Caroline. ·Oncology Research Institute, Loyola University Chicago, Maywood, Illinois. · Department of Chemistry and Biochemistry, The Harper Cancer Research Institute, University of Notre Dame, Notre Dame, Indiana. · Department of Dermatology, Lurie Comprehensive Cancer Center, Northwestern University, Chicago, Illinois. · Department of Microbiology and Immunology, Medical University of South Carolina, Charleston, South Carolina. · Department of Public Health Sciences, Medical University of South Carolina, Charleston, South Carolina. · Netherlands Institute for Pigment Disorders, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands. · Department of Dermatology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands. · Department of Surgery, Medical University of South Carolina, Charleston, South Carolina. · Department of Microbiology and Immunology, Northwestern University, Chicago, Illinois. ·Pigment Cell Melanoma Res · Pubmed #30009548.

ABSTRACT: To study the contribution of T-cell receptors (TCR) to resulting T-cell responses, we studied three different human αβ TCRs, reactive to the same gp100-derived peptide presented in the context of HLA-A*0201. When expressed in primary CD8 T cells, all receptors elicited classic antigen-induced IFN-γ responses, which correlated with TCR affinity for peptide-MHC in the order T4H2 > R6C12 > SILv44. However, SILv44 elicited superior IL-17A release. Importantly, in vivo, SILv44-transgenic T cells mediated superior antitumor responses to 888-A2 + human melanoma tumor cells upon adoptive transfer into tumor-challenged mice while maintaining IL-17 expression. Modeling of the TCR ternary complexes suggested architectural differences between SILv44 and the other complexes, providing a potential structural basis for the observed differences. Overall, the data reveal a more prominent role for the T-cell receptor in defining host T-cell physiology than traditionally assumed, while parameters beyond IFN-γ secretion and TCR affinity ultimately determine the reactivity of tumor-reactive T cells.

2 Article Clinical and immunologic evaluation of three metastatic melanoma patients treated with autologous melanoma-reactive TCR-transduced T cells. 2018

Moore, Tamson / Wagner, Courtney Regan / Scurti, Gina M / Hutchens, Kelli A / Godellas, Constantine / Clark, Ann Lau / Kolawole, Elizabeth Motunrayo / Hellman, Lance M / Singh, Nishant K / Huyke, Fernando A / Wang, Siao-Yi / Calabrese, Kelly M / Embree, Heather D / Orentas, Rimas / Shirai, Keisuke / Dellacecca, Emilia / Garrett-Mayer, Elizabeth / Li, Mingli / Eby, Jonathan M / Stiff, Patrick J / Evavold, Brian D / Baker, Brian M / Le Poole, I Caroline / Dropulic, Boro / Clark, Joseph I / Nishimura, Michael I. ·Department of Surgery, Loyola University Chicago, 2160 S. 1st Avenue, Maywood, IL, 60153, USA. tamoore@luc.edu. · Department of Medicine, Loyola University Chicago, 2160 S. 1st Avenue, Maywood, IL, 60153, USA. · Department of Surgery, Loyola University Chicago, 2160 S. 1st Avenue, Maywood, IL, 60153, USA. · Department of Pathology, Loyola University Chicago, 2160 S. 1st Avenue, Maywood, IL, 60153, USA. · Forefront Dermatology, 801 York St, Manitowoc, WI, 54220, USA. · O. Wayne Rollins Research Center, Emory University, Room 3127, 1510 Clifton Road NE, Atlanta, GA, 30322, USA. · Department of Chemistry & Biochemistry and the Harper Cancer Research Institute, University of Notre Dame, 251 Nieuwland Science Hall, Notre Dame, IN, 46656, USA. · Abbvie, 1 North Waukegan Road, North Chicago, IL, 60064, USA. · Lentigen Technology Inc, A Miltenyi Biotec Company, 910 Clopper Road Suite 200S, Gaithersburg, MD, 20878, USA. · Hollings Cancer Center, Medical University of South Carolina, 86 Jonathan Lucas St, Charleston, SC, 29425, USA. · Dartmouth-Hitchcock, Norris Cotton Cancer Center, One Medical Center Dr, Lebanon, NH, 03756, USA. · Department of Microbiology, and Immunology, Loyola University Chicago, 2160 S. 1st Avenue, Maywood, IL, USA. · Bluebird Biology, 60 Binney St., Cambridge, MA, 02142, USA. · Lurie Comprehensive Cancer Center, Department of Dermatology, Northwestern University at Chicago, Room 5-113, 303 East Superior Street, Chicago, IL, 60611, USA. ·Cancer Immunol Immunother · Pubmed #29052782.

ABSTRACT: Malignant melanoma incidence has been increasing for over 30 years, and despite promising new therapies, metastatic disease remains difficult to treat. We describe preliminary results from a Phase I clinical trial (NCT01586403) of adoptive cell therapy in which three patients received autologous CD4

3 Article FOXO3-NF-κB RelA Protein Complexes Reduce Proinflammatory Cell Signaling and Function. 2015

Thompson, Matthew G / Larson, Michelle / Vidrine, Amy / Barrios, Kelly / Navarro, Flor / Meyers, Kaitlyn / Simms, Patricia / Prajapati, Kushal / Chitsike, Lennox / Hellman, Lance M / Baker, Brian M / Watkins, Stephanie K. ·Cardinal Bernardin Cancer Center, Loyola University Chicago, Maywood, IL 60153; and. · Department of Chemistry and Biochemistry, Harper Cancer Research Institute, University of Notre Dame, Notre Dame, IN 46556. · Cardinal Bernardin Cancer Center, Loyola University Chicago, Maywood, IL 60153; and swatkins1@luc.edu. ·J Immunol · Pubmed #26561547.

ABSTRACT: Tumor-associated myeloid cells, including dendritic cells (DCs) and macrophages, are immune suppressive. This study demonstrates a novel mechanism involving FOXO3 and NF-κB RelA that controls myeloid cell signaling and impacts their immune-suppressive nature. We find that FOXO3 binds NF-κB RelA in the cytosol, impacting both proteins by preventing FOXO3 degradation and preventing NF-κB RelA nuclear translocation. The location of protein-protein interaction was determined to be near the FOXO3 transactivation domain. In turn, NF-κB RelA activation was restored upon deletion of the same sequence in FOXO3 containing the DNA binding domain. We have identified for the first time, to our knowledge, a direct protein-protein interaction between FOXO3 and NF-κB RelA in tumor-associated DCs. These detailed biochemical interactions provide the foundation for future studies to use the FOXO3-NF-κB RelA interaction as a target to enhance tumor-associated DC function to support or enhance antitumor immunity.

4 Article Genomic and bioinformatic profiling of mutational neoepitopes reveals new rules to predict anticancer immunogenicity. 2014

Duan, Fei / Duitama, Jorge / Al Seesi, Sahar / Ayres, Cory M / Corcelli, Steven A / Pawashe, Arpita P / Blanchard, Tatiana / McMahon, David / Sidney, John / Sette, Alessandro / Baker, Brian M / Mandoiu, Ion I / Srivastava, Pramod K. ·Department of Immunology and Carole and Ray Neag Comprehensive Cancer Center, University of Connecticut School of Medicine, Farmington, CT 06030. · Department of Computer Science and Engineering, University of Connecticut, Storrs, CT 06269. · Department of Chemistry and Biochemistry and Harper Cancer Research Institute, University of Notre Dame, Notre Dame, IN 46556. · LaJolla Institute of Allergy and Immunology, La Jolla, CA 92037. · Department of Computer Science and Engineering, University of Connecticut, Storrs, CT 06269 Srivastava@uchc.edu ion@engr.uconn.edu. · Department of Immunology and Carole and Ray Neag Comprehensive Cancer Center, University of Connecticut School of Medicine, Farmington, CT 06030 Srivastava@uchc.edu ion@engr.uconn.edu. ·J Exp Med · Pubmed #25245761.

ABSTRACT: The mutational repertoire of cancers creates the neoepitopes that make cancers immunogenic. Here, we introduce two novel tools that identify, with relatively high accuracy, the small proportion of neoepitopes (among the hundreds of potential neoepitopes) that protect the host through an antitumor T cell response. The two tools consist of (a) the numerical difference in NetMHC scores between the mutated sequences and their unmutated counterparts, termed the differential agretopic index, and (b) the conformational stability of the MHC I-peptide interaction. Mechanistically, these tools identify neoepitopes that are mutated to create new anchor residues for MHC binding, and render the overall peptide more rigid. Surprisingly, the protective neoepitopes identified here elicit CD8-dependent immunity, even though their affinity for K(d) is orders of magnitude lower than the 500-nM threshold considered reasonable for such interactions. These results greatly expand the universe of target cancer antigens and identify new tools for human cancer immunotherapy.

5 Article T-cell receptor specificity maintained by altered thermodynamics. 2013

Madura, Florian / Rizkallah, Pierre J / Miles, Kim M / Holland, Christopher J / Bulek, Anna M / Fuller, Anna / Schauenburg, Andrea J A / Miles, John J / Liddy, Nathaniel / Sami, Malkit / Li, Yi / Hossain, Moushumi / Baker, Brian M / Jakobsen, Bent K / Sewell, Andrew K / Cole, David K. ·Cardiff University School of Medicine, Heath Park, Cardiff CF14 4XN, United Kingdom. ·J Biol Chem · Pubmed #23698002.

ABSTRACT: The T-cell receptor (TCR) recognizes peptides bound to major histocompatibility molecules (MHC) and allows T-cells to interrogate the cellular proteome for internal anomalies from the cell surface. The TCR contacts both MHC and peptide in an interaction characterized by weak affinity (KD = 100 nM to 270 μM). We used phage-display to produce a melanoma-specific TCR (α24β17) with a 30,000-fold enhanced binding affinity (KD = 0.6 nM) to aid our exploration of the molecular mechanisms utilized to maintain peptide specificity. Remarkably, although the enhanced affinity was mediated primarily through new TCR-MHC contacts, α24β17 remained acutely sensitive to modifications at every position along the peptide backbone, mimicking the specificity of the wild type TCR. Thermodynamic analyses revealed an important role for solvation in directing peptide specificity. These findings advance our understanding of the molecular mechanisms that can govern the exquisite peptide specificity characteristic of TCR recognition.

6 Article T-cell receptor-optimized peptide skewing of the T-cell repertoire can enhance antigen targeting. 2012

Ekeruche-Makinde, Julia / Clement, Mathew / Cole, David K / Edwards, Emily S J / Ladell, Kristin / Miles, John J / Matthews, Katherine K / Fuller, Anna / Lloyd, Katy A / Madura, Florian / Dolton, Garry M / Pentier, Johanne / Lissina, Anna / Gostick, Emma / Baxter, Tiffany K / Baker, Brian M / Rizkallah, Pierre J / Price, David A / Wooldridge, Linda / Sewell, Andrew K. ·Institute of Infection and Immunity, Cardiff University School of Medicine, Henry Wellcome Building, Heath Park, Cardiff CF14 4XN, Wales, United Kingdom. ·J Biol Chem · Pubmed #22952231.

ABSTRACT: Altered peptide antigens that enhance T-cell immunogenicity have been used to improve peptide-based vaccination for a range of diseases. Although this strategy can prime T-cell responses of greater magnitude, the efficacy of constituent T-cell clonotypes within the primed population can be poor. To overcome this limitation, we isolated a CD8(+) T-cell clone (MEL5) with an enhanced ability to recognize the HLA A*0201-Melan A(27-35) (HLA A*0201-AAGIGILTV) antigen expressed on the surface of malignant melanoma cells. We used combinatorial peptide library screening to design an optimal peptide sequence that enhanced functional activation of the MEL5 clone, but not other CD8(+) T-cell clones that recognized HLA A*0201-AAGIGILTV poorly. Structural analysis revealed the potential for new contacts between the MEL5 T-cell receptor and the optimized peptide. Furthermore, the optimized peptide was able to prime CD8(+) T-cell populations in peripheral blood mononuclear cell isolates from multiple HLA A*0201(+) individuals that were capable of efficient HLA A*0201(+) melanoma cell destruction. This proof-of-concept study demonstrates that it is possible to design altered peptide antigens for the selection of superior T-cell clonotypes with enhanced antigen recognition properties.