St. Bonaventure University

Faculty


Schwingel, Johanna

schwingel-johanna

ACADEMIC DEPARTMENT
Biology
ACADEMIC SCHOOL
School of Arts and Sciences

TITLES/RESPONSIBILITIES
Associate Professor, Biology
Department Chair
CONTACT
Office phone: (716) 375-2639
Send an Email
OFFICE
Walsh Science Center 215
COURSES TAUGHT
  • BIOL 101: Fundamentals of Biology Lab
  • BIO/BIOL 321: General Microbiology Lecture and Lab
  • BIO/BIOL 472: Immunology Lecture and Lab
ACADEMIC DEGREES
  • Ph.D. in Microbiology and Immunology, University at Buffalo, 2009
  • B.S. in Genetic Engineering, Cedar Crest College, 2004
OTHER EDUCATION
  • Postdoctoral Research Associate, Department of Microbiology and Immunology, University of Rochester, 2009-2013 
PROFESSIONAL BACKGROUND
  • Adjunct Instructor for Microbiology at The College at Brockport (SUNY), Brockport, N.Y. 2013
  • Adjunct Instructor for Microbiology at Monroe Community College, Rochester, N.Y. 2011-2012
  • Adjunct Instructor for Microbiology and Human Disease at Genesee Community College, Batavia, N.Y. 2010-2011
ACCOMPLISHMENTS

Publications:

  • Schwingel, J. M. 2018. Exploring Infectious Disease Outbreaks and Herd Immunity Through Simulations with a Visual Appeal. Journal of Microbiology & Biology Education 19(2). doi.org/10.1128/jmbe.v19i2.1570.
  • Schwingel, J. M. 2018. Enhancing Scientific Communication Through an Undergraduate Biology and Journalism Partnership. Journal of Microbiology & Biology Education 19(1). doi: 10.1128/jmbe.v19i1.1445.
  • Tombline, G., J. M. Schwingel, J. Lapek, A. E. Friedman, T. Darrah, M. Maguire, N. E. Van Alst, M. J. Filiatrault, and B. H. Iglewski. 2013. Pseudomonas aeruginosa PA1006 Is a Persulfide-Modified Protein That Is Critical for Molybdenum Homeostasis. PLoS ONE 8(2): e55593. doi:10.1371/journal.pone.0055593.
  • Filiatrault M. J., G. Tombline, V. E. Wagner, N. E. Van Alst, K. Rumbaugh, P. Sokol, J. Schwingel, and B. H. Iglewski. 2013. Pseudomonas aeruginosa PA1006, Which Plays a Role in Molybdenum Homeostasis, Is Required for Nitrate Utilization, Biofilm Formation, and Virulence. PLoS ONE 8(2): e55594. doi:10.1371/journal.pone.0055594.
  • Canfield, G. S., J. M. Schwingel, M. H. Foley, K. L. Vore, K. Boonanantanasarn, A. L. Gill, M. D. Sutton, and S. R. Gill. 2013. Evolution in Fast Forward: A Potential Role for Mutators in Accelerating Staphylococcus aureus Pathoadaptation. Journal of Bacteriology 195(3): 615-628.
  • Schwingel, J. M., K. J. Edwards, A. D. Cox, H. Masoud, J. C. Richards, F. St. Michael, C. D. Tekwe, S. Sethi, T. F. Murphy, and A. A. Campagnari. 2009. The Use of Moraxella catarrhalis Lipooligosaccharide Mutants to Identify Specific Oligosaccharide Epitopes Recognized by Human Serum Antibodies. Infection and Immunity 77(10): 4548–4558.
  • Schwingel, J. M., F. St Michael, A. D. Cox, H. Masoud, J. C. Richards, and A. A. Campagnari. 2008. A unique glycosyltransferase involved in the initial assembly of Moraxella catarrhalis lipooligosaccharides. Glycobiology 18: 447-455.
  • Edwards, K. J., J. M. Schwingel, A. K. Datta, and A. A. Campagnari. 2005. Multiplex PCR Assay that Identifies the Major Lipooligosaccharide Serotype Expressed by Moraxella catarrhalis Clinical Isolates. Journal of Clinical Microbiology 43(12): 6139-6143.
TEACHING PHILOSOPHY
CURRENT RESEARCH INTERESTS/PROJECTS

Pseudomonas aeruginosa is a gram-negative bacterium that is ubiquitous in our environment. The bacterium causes chronic infections, however, it is of particular burden in cystic fibrosis and chronic obstructive pulmonary disease patients and is a major source of wound, burn, and hospital-acquired infections. P. aeruginosa uses many virulence factors, biofilms, and increased antibiotic resistance to contribute to disease.

A number of P. aeruginosa enzymes use molybdenum cofactor (MoCo), including nitrate reductase important for anaerobic growth and biofilm development. P. aeruginosa mutants unable to make MoCo have diminished biofilm development and reduced virulence in assays such as the Caenorhabditis elegans fast-kill assay, lettuce leaf model, and burned mouse model compared to the wild-type (Filiatrault et al. 2013. PLoS ONE. 8(2): e55594). Production of MoCo relies on a series of proteins to construct, assemble, and chaperone the cofactor to its conjugate enzymes.

Currently in my lab, we are investigating the cellular localization of the proteins involved in MoCo biosynthesis via bacterial mutant construction and a green fluorescent protein (GFP) fragment complementation assay to determine protein interactions. Students will have the opportunity to learn techniques such as bacterial culturing, basic bioinformatic analysis, PCR, general cloning methods, and fluorescence/confocal microscopy. In addition, we are also investigating P. aeruginosa mutants in different infection models to determine proteins involved in virulence or disease.

PERSONAL INTERESTS/COMMUNITY INVOLVEMENT
American Society for Microbiology (ASM) Member
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