Texas Biomed Staff

Andrew Hayhurst

Associate Scientist | Virology and Immunology
Phone: 210-258-9530
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In my laboratory we are developing disruptive technologies to detect and inhibit potentially lethal pathogens and toxins.  We are pursuing antibodies that are capable of recognizing a threat in a highly specific and sensitive manner that will be suitable for transition to biosensors and field portable diagnostics.  The spectrum of operating conditions these diagnostic tools face is enormous.  The harshest conditions are usually found in resource-poor areas of the world where electricity and refrigeration are rare and resupply is difficult.  Such areas require extremely rugged yet simple to operate single-use (dipstick) systems with long shelf-lives.  Harsh conditions still exist on the homeland front in a different way, because of the need for constant real-time environmental monitoring of biothreats in multiplex.  A highly promising antibody format with the potential to offer a solution to these problems is the single domain antibody (sdAb).

Using immune llama antibodies, we have been targeting the botulinum neurotoxins, the most poisonous substances currently known, estimated to be 100 billion times more toxic than cyanide.  We have succeeded in engineering a heptaplex assay to recognize the seven known serotypes of the neurotoxin based upon sdAb, all of which have proved to be suitable for making multiplex biosensor platforms more rugged.  We have also generated model assays from semi-synthetic llama sdAb that are specific for both Marburg virus and Ebola virus, which cause highly lethal hemorrhagic fevers in equatorial Africa.  Intriguingly, our semi-synthetic naïve anti-Ebola llama antibodies outperform immune shark antibodies, suggesting the potential for immune llama sdAb to yield even higher affinity clones to further improve the capacity for detection.  We are currently studying the molecular basis for recognition of the viral antigens by our sdAb in a collaboration with Alex Taylor and John Hart at the UTHSCSA crystallography core laboratory.

Recently, we have been focusing on ways to accelerate antibody selection, screening and assay assembly to formulate a low-tech, inexpensive antibody pipeline that can operate in basic laboratory environments to respond to any emerging threat with a stop-gap diagnostic assay.  I have invented a new screening process that rapidly identifies pairs of affinity reagents, including sdAb, without needing protein purification.  The basis for how the system works is engineering extracts from engineered E. coli to add a single molecule of biotin to the sdAb, splitting them to create “captors” and “tracers” and distinguishing between the two by temporally occluding the biotin.  The familiarity, speed and cost-effectiveness of the technology ensures affinity reagent pairing is very straightforward, requires no sophisticated equipment and accelerates the delivery of stop-gap assays to any given threat.

Our other interests include novel cancer therapeutics and nanotechnology.


Doctoral Degree: Ph.D. Virology (1995)

National Institute for Medical Research London , England

Bachelor's Degree B.S.

University of Reading , Reading , England

Postdoctoral Work

University of Aberdeen, Scotland, 1995-1998

University of Texas at Austin, TX, 1998-2000

Awards and Honors

2004    San Antonio Business Journal “40 under 40” award
2007    Naval Research Laboratory Alan Berman award for outstanding research publication, Facile generation of heat stable antiviral and antitoxin single domain antibodies from a semisynthetic llama library
2007 – NIH U01 Reviewer ZAI1-TP-M-J2, RFA-AI-07-003: Cooperative Research Partnerships in     Biodefense
2008 – NIH U01 Reviewer ZAI-1-3 (diagnostics) and ZAI-1-1 (immunotherapeutics), RFA-AI-08-001: Cooperative Research Partnerships in Biodefense
2009 – NIH P01 Reviewer, ZAI1 GPJ-M(S1):  Novel Diagnostics and Therapeutics for Caliciviruses
2009 – NIH Challenge Grant Reviewer ZRG1 IMM-E(58)R
2009 – Special Faculty Member, Graduate Program in Biology and Biotechnology, University of Texas at San Antonio
2010 – NIH R01 Reviewer ZAI1 FDS-M M2 1, RFA-AI-09-028:  Partnerships for Biodefense Viral Pathogens


USPO# US7,871,796 “Isolation of binding proteins with high affinity to ligands.”  UT Regents

Patent Pending, USPO#US 61/514,717 “Nucleic Acid Compositions, Methods and Kits for Rapid Ligand Pairing.” Texas Biomedical Research Institute


Ebolavirus nucleoprotein C-termini potently attract single domain antibodies enabling monoclonal affinity reagent sandwich assay (MARSA) formulation

Sherwood LJ, Hayhurst A.
PLoS One 8 (4): e61232, 2013
PubMed ID: 3618483

Hapten mediated display and pairing of recombinant antibodies accelerates assay assembly for biothreat countermeasures

Sherwood LJ, Hayhurst A.
Sci Rep 2: 807, 2012
PubMed ID: 3495282