Blythe Janowiak, Ph.D.
Associate Professor
Biology
Courses Taught
BIOL 3020: Biochemistry & Molecular Biology and BIOL 4160: Microbial Ecology & Molecular Evolution
Education
Ph.D., Medical College of Wisconsin
Research Interests
The Janowiak lab uses biochemistry, microbiology, and molecular genetics to explore the relationship between microbes and their environment. The lab has two main focuses:
1) Gram-positive pathogenic bacteria and their response to oxidative stresses produced by the mammalian host
Our bacterium of interest is Group B Streptococcus (Streptococcus agalactiae). Our favorite oxidative stress response is glutathione, and we specifically study its synthesis, import, export, and metabolism in the bacteria. To study the regulation of and the molecular mechanisms involved with glutathione metabolism, we are employing a combination of transcriptomics, metabolomics, and good old fashion biochemistry.
2) The contribution of glutathione and other antioxidants to the survival and maintenance of bacteria residing in the mouse vaginal microbiome
The lab is examining the effect of glutathione metabolism on the biodiversity of the
vaginal microbiota. Group B Streptococcus is often found in the healthy vaginal microbiome,
but can become an opportunistic pathogen and cause significant disease. Therefore, the
lab is interested in the role antioxidants, namely glutathione, play in maintaining
a healthy vaginal microbiome.
More information about the Janowiak Lab is available at
https://sites.google.com/a/slu.edu/janowiak-lab/
Labs and Facilities
The Janowiak lab, located in Macelwane Hall (room 221), welcomes graduate and undergraduate students in the laboratory with interest in the biochemistry of pathogenic bacteria. Research projects include the opportunity to study select Gram-positive pathogens using a variety of biochemical, microbiological, cellular, biophysical, and molecular techniques. Students interested are welcome to contact the lab about current research opportunities in the laboratory.
Publications and Media Placements
For the most up to date publications, please visit My Google Scholar Profile Page
Mannino MH, Patel RS, Eccardt AM, Janowiak BE, Wood DC, He F, Fisher JS. Reversible Oxidative Modifications in Myoglobin and Functional Implications. Antioxidants (Basel). 2020 Jun 24;9(6):E549. doi: 10.3390/antiox9060549. PMID: 32599765.
Eccardt AM, Pelzel RJ, Mattathil L, Moon YA, Mannino MH, Janowiak BE, Fisher JS. A peroxidase mimetic protects skeletal muscle cells from peroxide challenge and stimulates insulin signaling. Am J Physiol Cell Physiol. 2020 Jun 1;318(6):C1214-C1225. doi: 10.1152/ajpcell.00167.2019. Epub 2020 Apr 29. PMID: 32348172; PMCID: PMC7311744.
Walker EA, Port GC, Caparon MG, Janowiak BE. Glutathione Synthesis Contributes to Virulence of Streptococcus agalactiae in a Murine Model of Sepsis. J Bacteriol. 2019 Sep 20;201(20):e00367-19. doi: 10.1128/JB.00367-19. PMID: 31331978; PMCID: PMC6755738.
Mannino MH, Patel RS, Eccardt AM, Perez Magnelli RA, Robinson CLC, Janowiak BE, Warren DE, Fisher JS. Myoglobin as a versatile peroxidase: Implications for a more important role for vertebrate striated muscle in antioxidant defense. Comp Biochem Physiol B Biochem Mol Biol. 2019 Aug;234:9-17. doi: 10.1016/j.cbpb.2019.04.005. Epub 2019 Apr 30. PMID: 31051268; PMCID: PMC6594547.
Hixon KR, Lu T, Carletta MN, McBride-Gagyi SH, Janowiak BE, Sell SA. A preliminary in vitro evaluation of the bioactive potential of cryogel scaffolds incorporated with Manuka honey for the treatment of chronic bone infections. J Biomed Mater Res B Appl Biomater. 2018 Jul;106(5):1918-1933. doi:10.1002/jbm.b.34002. Epub 2017 Sep 27. PubMed PMID: 28960886.
Hixon KR, Lu T, McBride-Gagyi SH, Janowiak BE, Sell SA. A Comparison of Tissue Engineering Scaffolds Incorporated with Manuka Honey
of Varying UMF. Biomed Res Int. 2017;2017:4843065. doi: 10.1155/2017/4843065. Epub
2017 Feb 23. PubMed PMID:28326322; PubMed Central PMCID: PMC5343224.
Minden-Birkenmaier, B.A.; Neuhalfen, R.M.; Janowiak, B.E.; and Sell, S.A. Preliminary
Investigation and Characterization of Electrospun Polycaprolactone and Manuka Honey
Scaffolds for Dermal Repair. Journal of Engineered Fibers and Fabrics. 2015, Vol.
10 Issue 4, p126-138. 13p.
Akkaladevi, N., Mukherjee, S., Katayama, H., Janowiak, B.E., Patel, D., Gogol, E.P., Pentelute, B.L., John Collier, R., and Fisher, M.T. Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs. J Membr Biol. (2015) Jan 13. [Epub ahead of print] PMID: 25578459.
Rajapaksha, M., Lovell, S., Janowiak, B.E., Sun, J., Andra, K.K., Battaile, K.P., and Bann, J.G., pH effects on binding between
the anthrax protective antigen and the host cellular receptor CMG2. Protein Science.
21, 1467-1480 (2012).
Janowiak, B.E., Jennings-Antipov, L.D., and Collier, R.J., Cys-Cys crosslinking shows contact between the N-terminus of lethal factor and Phe427 within the anthrax toxin pore. Biochemistry. 50: 3512-3516 (2011).
Wimalasena, D.S., Janowiak, B.E., Lovell, S., Miyagi, M., Sun, J., Zhou, H., Hajduch, J., Pooput, C., Kirk, K.L., Battaile, K.P., Bann, J.G., Evidence That Histidine Protonation of Receptor-Bound Anthrax Protective Antigen Is a Trigger for Pore Formation. Biochemistry. 49: 6973-6983 (2010).
Zornetta, I., Brandi, L., Janowiak, B., Dal Molin, F., Tonello, F., Collier, R.J., Montecucco, C., Imaging the cell entry of the anthrax oedema and lethal toxins with fluorescent protein chimeras. Cell Microbiol. 12: 1435-1445 (2010).
Pentelute BL, Barker AP, Janowiak BE, Kent SB, Collier RJ., A semisynthesis platform for investigating structure-function relationships in the N-terminal domain of the anthrax Lethal Factor. ACS Chem Biol. 2010 Apr 16;5(4):359-64.
Janowiak BE*, Fischer A*, Collier RJ., Effects of introducing a single charged residue into the
phenylalanine clamp of multimeric anthrax protective antigen. J Biol Chem. 2010 Mar
12;285(11):8130-7. Epub 2010 Jan 8.
*both authors contributed equally
Nakashima Y, Nii H, Janowiak BE, Griffith OW, Hibi T., Crystallization and preliminary crystallographic analysis of bifunctional gamma-glutamylcysteine synthetase-glutathione synthetase from Streptococcus agalactiae. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt 7):678-80. Epub 2009 Jun 27.
Janowiak BE, Finkelstein A, Collier RJ., An approach to characterizing single-subunit mutations in multimeric prepores and pores of anthrax protective antigen. Protein Sci. 2009 Feb;18(2):348-58.
Katayama H*, Janowiak BE*, Brzozowski M, Juryck J, Falke S, Gogol EP, Collier RJ, Fisher MT., GroEL as a molecular
scaffold for structural analysis of the anthrax toxin pore., Nat Struct Mol Biol.
2008 Jul;15(7):754-60. Epub 2008 Jun 22.
*both authors contributed equally
Wimalasena DS, Cramer JC, Janowiak BE, Juris SJ, Melnyk RA, Anderson DE, Kirk KL, Collier RJ, Bann JG., Effect of 2-fluorohistidine labeling of the anthrax protective antigen on stability, pore formation, and translocation. Biochemistry. 2007 Dec 25;46(51):14928-36. Epub 2007 Nov 29.
Janowiak BE, Hayward MA, Peterson FC, Volkman BF, Griffith OW., Gamma-glutamylcysteine synthetase-glutathione synthetase: domain structure and identification of residues important in substrate and glutathione binding. Biochemistry. 2006 Sep 5;45(35):10461-73.
Janowiak BE, Griffith OW., Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities. J Biol Chem. 2005 Mar 25;280(12):11829-39. Epub 2005 Jan 10.
Brenot A, King KY, Janowiak B, Griffith O, Caparon MG., Contribution of glutathione peroxidase to the virulence
of Streptococcus pyogenes.
Infect Immun. 2004 Jan;72(1):408-13.