Research | Lab Members | SFBR.org
Andrew Hayhurst, Ph.D.
Texas Biomedical Research InstituteDepartment of Virology and Immunology
Tel: (210) 258-9530Fax: (210) 58-339Email:
Our laboratory has a variety of interests mostly related to antibody engineering technology and applications to emerging pathogen countermeasures, tumor targeting and nanotechnology. We have recently developed a simple yet effective route to transition from large antibody repertoires to individual sandwich assays in a single day without the need for protein purification or modification to accelerate the antibody characterization process. The rapid antibody pipeline was used to formulate an anti-botulinum neurotoxin assay from an immune repertoire and an anti-Zaire Ebolavirus assay from a non-immune library within the BSL4 lab. We continue to explore the molecular basis for antigen recognition by llama single domain antibodies with our collaborators Alex Taylor and John Hart (UTHSCSA) to rationalize why our antibodies are so effective at recognizing Filovirus nucleoprotein C-termini thereby enabling monoclonal affinity reagent sandwich assays to function so well. As part of this work we are developing a high throughput system to deconvolute the amino-acid residues within both antigen and antibody that are critical for recognition to complement the structural approach and help when antibody-antigen complexes prove fickle to crystallize. We are aiming to disrupt the Filoviral replication machinery using single domain antibodies as intrabodies since they can be potent inhibitors of specific roles of multifunctional proteins and enable one to break down individual contributions to the viral life cycle as opposed to siRNA knockdown style experiments. Our tumor targeting work involves modifying bacterial surfaces to more homogenously target tumors rather than just necrotic cores in order to enhance the likelihood of complete tumor regression following bacterial based therapies. Our in interests in nanotechnology center on an unusual protein format that appears to rapidly stimulate the promiscuous formation of macromolecular crystalline aggregates of several salts that are visible to the naked eye and we hope to rationalize the mechanism of this phenomenon.