Catherine Schein is a Professor in the Department of Biochemistry and Molecular Biology at the University of Texas Medical Branch (UTMB) in Galveston, Texas. She received her academic training at the University of Pennsylvania, Massachusetts Institute of Technology, and the ETH in Zürich, Switzerland. She remained in Zürich after her PhD to begin a postdoc with Dr. Charles Weissmann on expression of recombinant human interferons, which led to her first position at Biogen SA, as director of the first large-scale production of these proteins. After transferring the process to Schering Plough in New Jersey, she returned to research on producing recombinant growth factors and cytokines solubly and studying their structure and function. She began this research at Biogen and then as an Oberassistentin  at the ETH- Zürich, working with Dr. Tim Richmond in crystallography and Dr. Stephen Benner in Organic Chemistry. She was funded in the latter position by a young faculty grant from the Zȕrcher Krebsliga (Cancer Society).   After moving to Texas with her family, she became an Assistant and Associate Professor at the University of Texas Medical Branch. In 2013, she became a Senior Fellow at the Foundation for Molecular Evolution (FfAME) in Florida, to conduct research on inhibitors of the polymerases of polio and other enteroviruses. She returned to the UTMB in 2018 and was promoted to Professor in the Department of Biochemistry and Molecular Biology in 2024, with a secondary appointment in the Department of Microbiology and Immunology.

Her research on virus proteins and allergens has been funded by grants from several agencies, including the NIH and the US EPA. She has served on review panels and study sections for the NIH and NSF. She is a member of HESI/PATB (Health and Environmental Studies Institute/Committee on Protein Allegens, Toxins and Bioinformatics, whose purpose is to assess the potential allergenicity and toxicity of novel plant products.

The long-term goal of Dr. Schein’s research is to understand the molecular mechanisms by which proteins cause disease, identifying the epitopes of allergenic and viral proteins. She is also using novel bioinformatic tools to access the information underlying data from genomics, proteomics and metabolomics databases to facilitate new design of vaccines, diagnostics and treatments for allergy and viral disease. 

Specific Projects

(1)Physicochemical property consensus (PCPcon) of viruses and allergens. 

This tool was developed to design rational reference sequences. We have shown it can also help in designing vaccines and inhibitors of the plus strand RNA viruses, alphaviruses (including eastern ,western and Venezuelan encephalitis viruses (EEEV, WEEV, VEEV) and Chikungunya (CHIKV)) and flaviviruses (such as Dengue (DENV), Zika and Yellow fever). When assembling our Flavitrack database, we found the ‘reference strain’ for groups of flaviviruses was often very old. To design more rational reference sequences that would better account for current strains, we derived the “PCPcon” method. Here, the amino acids in each column of aligned sequences were analyzed according to their PCPs, and the PCP values for each type of amino acids that could occur at that position was averaged.  We showed that the PCPcon calculated sequence was more identical to each sequence in a group than they were to each other.  

2) Broad spectrum, protein based vaccines and diagnostics for DENV and alphaviruses

Differing serotypes of viruses arise when the sequence, typically of surface areas, mutates sufficiently to react differently with the immune system. The envelope proteins of the four main DENV serotypes differ in sequence identity by ~40%; that of CHIKV differs from encephalitic alphaviruses by about 60%.   We have found that the PCPcon protein of even very diverse viruses can be recognized by sera from animals and people infected by individual viruses, that they fold similarly to individual wild type proteins, they induce antibodies in sera of rabbits and mice that are broadly neutralizing, and, as a vaccine, can protect/lower viremia against pathogenic alphaviruses in a murine model.  We are further developing them as the basis of broad-spectrum diagnostics and vaccines.

(3) Structural biology of allergens. Understanding the similar structure and properties of types of allergenic proteins is important for detecting potentially cross-reacting proteins, assays to help in treatment of patients, reducing allergens in our food and air, and eventually for designing hypoallergenic proteins for use in foods and immunotherapy. UTMB was home to the first cross referenced data base of allergenic proteins, the Structural Database of Allergenic Proteins, or SDAP. Many tools have been incorporated into SDAP to visualize the structure and common properties of these proteins and the areas identified as epitopes, based on experimental data. We are using SDAP tools and experimentally documented IgE epitopes to design conformationally constrained peptides to make diagnostics more precise and perhaps serve in improving peptide immunotherapy or as inhibitors of severe responses to nut allergens.

(4) The conditional nature of protein toxicity. Together with the Braun group at UTMB and members of HESI, we initiated a database of protein toxins and validated methods to rapidly assess the similarity of a novel protein to these known toxins. As with SDAP, this toxin database could help assess the toxicity of novel proteins and design novel inhibitors.

Some natural proteins are extremely potent toxins (e.g. ricin, tetanus and botulinus toxins) yet still have uses in lab assays, vaccines, removing wrinkles, and even breaking down the acrylamide in potato chips and other fried food. Other essential proteins, interferons and cytokines (e.g. tumor necrosis factor), are implicated in overreaction to pathogens, arthritis and autoimmune syndromes.  Foods that are innocuous to most of the population, such as peanuts, shrimp, eggs, or gluten containing foods, may cause severe reactions in sensitive individuals.  My recent book, Conditionally Toxic Proteins (www.routledge.com/9781032366937), explores some ways that proteins can become toxic, by inducing an immune response, or through mutation or aggregation.  

See https://scholar.google.com/citations?user=asBOBhgAAAAJ&hl=en for related references.