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Search Publications by: D. Travis Gallagher (Fed)

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Displaying 1 - 25 of 108

Effects of Glycans and Hinge on Dynamics in the IgG1 Fc

October 28, 2023
Author(s)
Christina Bergonzo, J. Todd Hoopes, Zvi Kelman, David Travis Gallagher
The crystallizable fragment (Fc) domain of immunoglobulin subclass IgG1 antibodies is engineered for a wide variety of pharmaceutical applications. Two important structural variables in Fc constructs are the hinge region connecting the Fc to the antigen

SARS-CoV-2 infection establishes an enhanced, stable, and age-independent CD8+ T cell response against a dominant nucleocapsid epitope using highly restricted TCRs

October 23, 2023
Author(s)
Cecily Choy, Joseph Chen, Jiangyuan Li, Jian Lu, Daichao Wu, Ainslee Zou, Humza Hemani, Beverly Baptiste, Emily Wichmann, Qian Yang, Jeffrey Ciffelo, Rui Yin, Julia McKelvy, Denise Melvin, Tonya Wallace, Christopher Dunn, Cuong Nguyen, Chee Chia, Jingshui Fan, Jeannie Ruffolo, Linda Zukley, Guixin Shi, Tomokazu Amano, An Yang, Osorio Meirelles, Wells Wu, Rong-Fong Chen, RICHARD WILLIS, Minoru Ko, Y-T Liu, Supriyo De, Brian Pierce, Luigi Ferrucci, josephine egan, Roy Mariuzza, Nan-ping Weng, David Travis Gallagher
We analyzed circulating CD8+ T cells recognizing six epitopes from the SARS-CoV-2 nucleocapsid (N) protein in HLA-A2+ unexposed and recovered COVID-19 patients using multi-color flow cytometry and scRNAseq. We found that SARS-CoV-2 infection slightly

Design and characterization of a protein fold switching network

January 26, 2023
Author(s)
David Travis Gallagher, Biao Ruan, Yanan He, Yingwei Chen, Eun Jung Choi, Yihong Chen, Dana Motabar, Tsega Solomon, Richard Simmerman, Thomas Kauffman, John Orban, Philip Bryan
Protein sequences encoding three common small folds (3-alpha, beta-grasp, and alpha/beta plait) were connected in a network of mutational pathways that intersect at high-identity sequences, termed nodes. The structures of proteins around nodes were

Crystal Structure of a Bivalent Antibody Fab Fragment

November 11, 2020
Author(s)
Salman Shahid, Mingming Gao, David Travis Gallagher, Steven Foung, Zhen-Yong Keck, Thomas Fuerst, Roy Mariuzza
We determined the crystal structure to 1.8 Å resolution of the Fab fragment of an affinity- matured human monoclonal antibody (HC84.26.5D) that recognizes the E2 envelope glycoprotein of hepatitis C virus (HCV). Unlike conventional Fabs, which are

Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen

June 9, 2020
Author(s)
David Travis Gallagher, Roy A. Mariuzza, Brian G. Pierce, Daichao Wu, Ragul Gowthaman
Abstract Adoptive cell therapy (ACT) with tumor-specific T cells can mediate cancer regression. The main target of tumor-specific T cells are neoantigens arising from mutations in self-proteins. Although the majority of cancer neoantigens are unique to

Structure of the Fc Fragment from the NIST Reference Antibody RM8671

September 1, 2018
Author(s)
David Travis Gallagher, Connor V. Galvin, Ioannis Karageorgos
As the link between antigen binding and immune activation, the antibody Fc region has received extensive structural study. In this report, the structure of the Fc fragment of the NIST IgG1 mAb (reference material 8671) is described at 2.1 Å resolution in

Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

December 1, 2017
Author(s)
Darion Spigolon, David Travis Gallagher, Adrian Velazquez-Campoy, Donatella Bulone, Jatin Narang, Pier San Biagio, Francesco Cappello, Alberto J. Macario, Everly Conway de Macario, Frank Robb
The human chaperonin complex is a 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy

A Bacteriophage Endolysin that Eliminates Intracellular Streptococci

March 15, 2016
Author(s)
Yang Shen, Marilia Barros, Tarek Vennemann, David Travis Gallagher, Yizhou Yin, Sara B. Linden, Ryan D. Heselpoth, Dennis J. Spencer, David M. Donovan, John Moult, Vincent A. Fischetti, Frank Heinrich, Mathias Loesche, Daniel C. Nelson
PlyC, a bacteriophage-encoded A-B endolysin, lyses Streptococcus pyogenes (Spy) on contact and protects mice from upper respiratory Spy colonization. Here, we demonstrate that PlyC is a novel, potent agent for targeting and controlling intracellular Spy
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