Matthieu G. Gagnon, PhD

Matthieu G. Gagnon, PhD

Assistant Professor, Department of Microbiology & Immunology

Tel: (409) 772-2326
Fax: (409) 772-2366
E-mail: magagnon@utmb.edu
Campus Location: 4.104C Medical Research Bldg
Mail Route: 1019

Pubmed Publications


Our research focuses on structural studies of protein synthesis, ribosome structure and function, ribosome-binding factors, antibiotics, antibiotic resistance mechanisms, X-ray crystallography, cryo-electron microscopy.

Current Projects

The increasing occurrence of bacterial resistance to antibiotics ranks among the greatest threats currently facing human health. The severity of the situation is such that it is propelling the search for new and more effective therapeutics. Antibiotics inhibit bacterial growth by targeting essential cellular processes such as cell wall synthesis, DNA replication/transcription and protein synthesis. Protein synthesis is mediated by a large macromolecular machine, called the ribosome. Nowadays, more than half of clinically relevant antibiotics cure infections by binding and inhibiting the bacterial ribosome, making the ribosome a validated drug target in the cell.

The fast up rise of drug-resistant pathogens and the threat that it poses to humanity warrant the pressing need to bring to the market new and improved compounds that target the bacterial ribosome. Over the past fifteen years, high-resolution structures of the ribosome have been determined at several points along the translation pathway, providing insights into decoding, translocation, termination, and the mechanisms by which many antibiotics inhibit protein synthesis. We are interested in understanding the mechanisms of protein synthesis and the basic cellular processes regulating translation by elucidating atomic structures of ribosome, RNA and protein functional complexes.

One of the ongoing projects in our laboratory focuses on the molecular mechanisms by which bacterial pathogens gain resistance to ribosome-targeting antibiotics. Of particular interest are the ribosome rescue factors that bind antibiotic-stalled ribosomes and allow pathogenic bacteria to resume protein synthesis and thrive in the presence of drugs. We seek to obtain tri-dimensional complex structures of the ribosome bound to specialized rescue factors, which will extend our current understanding of the molecular mechanisms that contribute to antibiotic resistance against ribosome-targeting antibiotics in many human pathogens. The availability of high-resolution structures is expected to assist in the design of smarter drugs capable of fighting antibiotic resistance. To achieve these goals, we are using an integrated approach combining biochemical, biophysical, genomic, molecular genetics and structure determination techniques.

We are always looking for highly motivated individuals who are interested in joining our dynamic and fast growing research group.