Travis Gallagher

Research Chemist

Gallagher Group

Contact

Email: dgallag1@umd.edu

Call: (240) 314-6204

Education

  • Ph.D., Chemistry, University of Texas at Austin, 1990      
  • B.S., Electrical Engineering and Computer Science, MIT, 1979

Profile

 

        Dr. Travis Gallagher’s research combines crystallography with other measurements and modeling strategies to provide structural descriptions of proteins and their interactions. Three major current foci are antibodies, vaccines and T cell receptors.

 

CURRENT RESEARCH

Antibody Structure

        The NIST standard antibody (reference material 8671, also called NISTmAb), has become a widely used industry standard, largely because of its extensive characterization at IBBR and at NIST. Dr. Gallagher has produced crystal structures of both the Fab and Fc fragments, and combined them with other information to generate an all-atom structural model of this IgG1 antibody. The pdb format model contains all 1326 amino acids in four chains, plus complete G1F/G0F glycans, and is available from data.nist.gov, along with the associated publication. The model is useful for conformational study of its biological signaling complexes (see Figure) and as a starting point for molecular dynamics. A long-term goal is to map the conformational space of the antibody to better understand its range and dimensionality, and to address the relation between conformation and biologically important phenomena like aggregation and signaling.

 

Vaccines and T Cell Receptors

        Bacterial proteins tend to stimulate the human immune system and have been used as components in several successful vaccine constructs. With material provided by a local vaccine research and development company, Dr. Gallagher has solved the first structure of a monomeric CRM-197 from Corynebacterium diphtheriae. The structure enables modeling of the dimerization process and will be useful for carrier-based vaccine strategies generally.

        T cell receptors (TCR) that bind to antigens from SARS-CoV-2 are the focus of a current ‘Seed Grant’ collaboration among IBBR researchers Mariuzza, Pierce, and Gallagher. In this work, crystal structures of TCR complexes with viral epitopes presented by MHC molecules are determined in order to advance understanding of how T cells contribute to defenses against this pandemic virus. While dozens of antibodies that bind the SARS-CoV-2 spike protein have been structurally characterized, comparatively little is known about the corresponding T cell responses, which include reactions against non-spike proteins from within the virus.      

Publications
2020
Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen.
2019
Structure and Dynamics of a Site-Specific Labeled Fc Fragment with Altered Effector Functions.
A Quality Improvement Approach to Increase Exercise Assessment in Survivors of Childhood Leukemia.
2018
Structure of the Fc fragment of the NIST reference antibody RM8671.
Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog.
Characterization of the NISTmAb Reference Material using small-angle scattering and molecular simulation : Part I: Dilute protein solutions.
2017
Biophysical characterization and structure of the Fab fragment from the NIST reference antibody, RM 8671.
2016
A bacteriophage endolysin that eliminates intracellular streptococci.
2015
Stray light correction in the optical spectroscopy of crystals.
2014
Membrane protein resistance of oligo(ethylene oxide) self-assembled monolayers.
2012
X-ray crystal structure of the streptococcal specific phage lysin PlyC.
On the need for an international effort to capture, share and use crystallization screening data.
2011
Solution NMR evidence for symmetry in functionally or crystallographically asymmetric homodimers.
2010
Active-site structure of class IV adenylyl cyclase and transphyletic mechanism.
Protein Crystal Engineering of YpAC-IV using the Strategy of Excess Charge Reduction.
2009
Structure of a switchable subtilisin complexed with a substrate and with the activator azide.
Profound asymmetry in the structure of the cAMP-free cAMP Receptor Protein (CRP) from Mycobacterium tuberculosis.
The Biomolecular Crystallization Database Version 4: expanded content and new features.
2008
Structure and lability of archaeal dehydroquinase.
Engineering substrate preference in subtilisin: structural and kinetic analysis of a specificity mutant.