Michael Baldwin, PhD's laboratory is focused on understanding how bacterial pathogens cause disease in the human population. In particular, he is studying botulinum neurotoxins, soluble proteins that readily diffuse from the site of infection to alter neuronal cell function with damaging effects on the intoxicated individual. The central theme of his research is to understand the molecular basis of protein translocation, the process by which the toxin catalytic domain is transported across the endosomal membrane bilayer to the cell cytosol. To pursue this goal, he has developed new spectroscopic and biochemical approaches to study the insertion of toxin into the membrane, which suggest that formation of the membrane-spanning channel involves discrete membrane binding and membrane insertion steps. While the extreme potency of the botulinum toxins poses a severe risk to human health, the highly specific targeting of nerve cells has also enabled their use as effective drugs to treat over 100 human maladies. Thus, investigations into the basic molecular mechanisms of botulinum toxin function has the potential to yield novel therapeutics against intoxication and improve and expand upon the current clinical uses of these molecules.
M618 Medical Sciences Bldg
Columbia, MO 65212
- Bacterial pathogenesis
- Membrane biochemistry
- Structural biology
Areas of Expertise
- Bacterial Pathogenesis
Education & Training
1998, PhD, University of London, UK
- Burns JR, Lambert GS, Baldwin MR. Insights into the Mechanisms by Which Clostridial Neurotoxins Discriminate between Gangliosides. Biochemistry. 2017;56(20):2571-83. doi: 10.1021/acs.biochem.6b01246. PubMed PMID: 28441004.
- Lea WA, O'Neil PT, Machen AJ, Naik S, Chaudhri T, McGinn-Straub W, Tischer A, Auton MT, Burns JR, Baldwin MR, Khar KR, Karanicolas J, Fisher MT. Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins. Biochemistry. 2016;55(35):4885-908. doi: 10.1021/acs.biochem.6b00293. PubMed PMID: 27505032.
- Lambert GS, Baldwin MR. Evidence for dual receptor-binding sites in Clostridium difficile toxin A. FEBS letters. 2016;590(24):4550-63. doi: 10.1002/1873-3468.12487. PubMed PMID: 27861794.
- Manse JS, Baldwin MR. Binding and entry of Clostridium difficile toxin B is mediated by multiple domains. FEBS letters. 2015;589(24 Pt B):3945-51. doi: 10.1016/j.febslet.2015.11.017. PubMed PMID: 26602083.
- Burns JR, Baldwin MR. 2014. Tetanus neurotoxin utilizes two sequential membrane interactions for channel formation. The Journal of biological chemistry. 2014;289(32):22450-8. doi: 10.1074/jbc.M114.559302. PubMed PMID: 24973217; PMCID: PMC4139251.