About

Jeniel Nett is a faculty member in the Division of Infectious Disease at the Department of Medicine, University of Wisconsin–Madison. She is part of a division that focuses on infectious disease research and clinical programs. The division is led by Division Chief David Andes, MD, with Associate Clinical Chief Christopher Saddler, MD, and APP Supervisor Paula Cynkar, PA. The division's work encompasses clinical research, innovative clinical programs, and multidisciplinary collaboration. Specific details about her research focus, background, or key contributions are not provided on the page.

Research topics

• Biology
• Microbiology
• Genetics
• Cell biology
• Biochemistry
• Immunology
• Botany
• Medicine
• Intensive care medicine
• Ecology

Selected publications

• Candida auris skin colonization is mediated by Als4112 and interactions with host extracellular matrix proteins

  Open MIND · 2026-02-17

  article

  <i>Candida auris</i> is an often multidrug-resistant fungal pathogen notorious for persistent skin colonization and transmission in healthcare settings. However, the mechanisms driving its adherence to skin remain poorly understood. Here, we developed <i>in vitro</i> systems to allow for detailed analysis of early skin colonization events and identified critical host and pathogen mediators of attachment. Across multiple strains and clades of <i>C. auris,</i> we identified that Als4112, a conserved adhesin, is required for skin colonization via keratinocyte attachment and direct interactions with host extracellular matrix (ECM) proteins, especially basement membrane proteins such as laminin. In a murine epicutaneous infection and human skin explants, deletion of <i>ALS4112</i> significantly reduced skin colonization, underscoring its essential role in establishing cutaneous persistence. Als4112 also contributes to systemic infection, highlighting the connection between adherence and pathogenicity in this organism. Finally, coating plastic and catheter surfaces with collagen I or III markedly inhibited <i>C. auris</i> attachment and biofilm formation, offering an approach to curb nosocomial transmission. Our study highlights the critical role of Als4112 in <i>C. auris</i> colonization and virulence <i>in vivo</i>, making it an attractive target for future vaccine development. This study also explores the potential of specific collagen coatings as a novel strategy to prevent <i>C. auris</i> adherence to abiotic surfaces, offering new therapeutic avenues to control the spread of <i>C. auris</i> in healthcare settings.

  DOI

• Trk1 potassium transport is crucial for effective <i>Candidozyma auris</i> skin colonization

  Proceedings of the National Academy of Sciences · 2026-04-21

  articleOpen accessSenior author

  The recently emergent fungal pathogen Candidozyma (Candida) auris has produced numerous outbreaks of invasive disease in hospitals worldwide. It is the first fungal pathogen categorized as a global public health threat due to its ability to readily colonize skin, spread efficiently person-to-person, and cause invasive infection with high mortality. Skin colonization not only promotes healthcare spread but also leads to invasive infection via the insertion of medical devices through skin. However, the mechanisms underlying C. auris survival in the skin niche remain poorly understood. Here, we identify potassium (K + ) as a crucial nutrient for efficient growth in this environment. We show that putative high-affinity K + transporter Trk1 is required for C. auris growth on human skin ex vivo. Disruption of TRK1 significantly impairs K + uptake and leads to plasma membrane hyperpolarization, a lower intracellular pH, and sensitivity to cationic stress. These findings demonstrate that TRK1 is necessary for maintaining K + homeostasis during C. auris colonization of human skin, shedding light on pathogenesis for this emerging threat. Given that TRK1 has no known human homologs, the gene product may serve as a promising therapeutic target for development of novel strategies directed at C. auris propagating on skin.

  PublisherOA PDFDOI

• Adhesin Als4112 promotes Candida auris skin colonization through interactions with keratinocytes and extracellular matrix proteins.

  Health Research Alliance · 2026-02-17

  articleOpen access

  Candida auris is a fungal pathogen notorious for persistent skin colonization and transmission in healthcare settings. Here, we show that a C. auris conserved adhesin, Als4112, is required for skin colonization via keratinocyte attachment and direct interactions with host extracellular matrix proteins, especially basement membrane proteins such as laminin. Deletion of ALS4112 reduces skin colonization in mouse models of epicutaneous and systemic infection. In addition, coating plastic and catheter surfaces with collagen I or III inhibits C. auris attachment and biofilm formation. Our study highlights the critical role of Als4112 in C. auris colonization and virulence, and explores potential strategies to reduce the pathogen’s adherence to abiotic surfaces and thus its spread in healthcare settings.

  PublisherDOI

• In Vivo Characterization of Candida Extracellular Vesicles Reveals Unique Infection Pathway Proteins

  JCI Insight · 2026-04-23

  articleOpen access
  PublisherOA PDFDOI

• A Candida auris-specific adhesin, Scf1, governs surface association, colonization, and virulence

  Health Research Alliance · 2026-02-17

  articleOpen access

  Candida auris is an emerging fungal pathogen responsible for health care–associated outbreaks that arise from persistent surface and skin colonization. We characterized the arsenal of adhesins used by C. auris and discovered an uncharacterized adhesin, Surface Colonization Factor (Scf1), and a conserved adhesin, Iff4109, that are essential for the colonization of inert surfaces and mammalian hosts. SCF1 is apparently specific to C. auris, and its expression mediates adhesion to inert and biological surfaces across isolates from all five clades. Unlike canonical fungal adhesins, which function through hydrophobic interactions, Scf1 relies on exposed cationic residues for surface association. SCF1 is required for C. auris biofilm formation, skin colonization, virulence in systemic infection, and colonization of inserted medical devices.

  PublisherDOI

• A Candida auris-specific adhesin, Scf1, governs surface association, colonization, and virulence

  Health Research Alliance · 2026-02-17

  articleOpen access

  Candida auris is an emerging fungal pathogen responsible for health care–associated outbreaks that arise from persistent surface and skin colonization. We characterized the arsenal of adhesins used by C. auris and discovered an uncharacterized adhesin, Surface Colonization Factor (Scf1), and a conserved adhesin, Iff4109, that are essential for the colonization of inert surfaces and mammalian hosts. SCF1 is apparently specific to C. auris, and its expression mediates adhesion to inert and biological surfaces across isolates from all five clades. Unlike canonical fungal adhesins, which function through hydrophobic interactions, Scf1 relies on exposed cationic residues for surface association. SCF1 is required for C. auris biofilm formation, skin colonization, virulence in systemic infection, and colonization of inserted medical devices.

  PublisherDOI

• Candida auris skin colonization is mediated by Als4112 and interactions with host extracellular matrix proteins

  Health Research Alliance · 2026-02-17

  articleOpen access

  <i>Candida auris</i> is an often multidrug-resistant fungal pathogen notorious for persistent skin colonization and transmission in healthcare settings. However, the mechanisms driving its adherence to skin remain poorly understood. Here, we developed <i>in vitro</i> systems to allow for detailed analysis of early skin colonization events and identified critical host and pathogen mediators of attachment. Across multiple strains and clades of <i>C. auris,</i> we identified that Als4112, a conserved adhesin, is required for skin colonization via keratinocyte attachment and direct interactions with host extracellular matrix (ECM) proteins, especially basement membrane proteins such as laminin. In a murine epicutaneous infection and human skin explants, deletion of <i>ALS4112</i> significantly reduced skin colonization, underscoring its essential role in establishing cutaneous persistence. Als4112 also contributes to systemic infection, highlighting the connection between adherence and pathogenicity in this organism. Finally, coating plastic and catheter surfaces with collagen I or III markedly inhibited <i>C. auris</i> attachment and biofilm formation, offering an approach to curb nosocomial transmission. Our study highlights the critical role of Als4112 in <i>C. auris</i> colonization and virulence <i>in vivo</i>, making it an attractive target for future vaccine development. This study also explores the potential of specific collagen coatings as a novel strategy to prevent <i>C. auris</i> adherence to abiotic surfaces, offering new therapeutic avenues to control the spread of <i>C. auris</i> in healthcare settings.

  PublisherDOI

• Adhesin Als4112 promotes Candida auris skin colonization through interactions with keratinocytes and extracellular matrix proteins.

  Health Research Alliance · 2026-02-17

  articleOpen access

  Candida auris is a fungal pathogen notorious for persistent skin colonization and transmission in healthcare settings. Here, we show that a C. auris conserved adhesin, Als4112, is required for skin colonization via keratinocyte attachment and direct interactions with host extracellular matrix proteins, especially basement membrane proteins such as laminin. Deletion of ALS4112 reduces skin colonization in mouse models of epicutaneous and systemic infection. In addition, coating plastic and catheter surfaces with collagen I or III inhibits C. auris attachment and biofilm formation. Our study highlights the critical role of Als4112 in C. auris colonization and virulence, and explores potential strategies to reduce the pathogen’s adherence to abiotic surfaces and thus its spread in healthcare settings.

  PublisherDOI

• Adhesin Als4112 promotes Candida auris skin colonization through interactions with keratinocytes and extracellular matrix proteins

  Nature Communications · 2025-07-01 · 17 citations

  articleOpen access

  Candida auris is a fungal pathogen notorious for persistent skin colonization and transmission in healthcare settings. Here, we show that a C. auris conserved adhesin, Als4112, is required for skin colonization via keratinocyte attachment and direct interactions with host extracellular matrix proteins, especially basement membrane proteins such as laminin. Deletion of ALS4112 reduces skin colonization in mouse models of epicutaneous and systemic infection. In addition, coating plastic and catheter surfaces with collagen I or III inhibits C. auris attachment and biofilm formation. Our study highlights the critical role of Als4112 in C. auris colonization and virulence, and explores potential strategies to reduce the pathogen’s adherence to abiotic surfaces and thus its spread in healthcare settings. Candida auris is a fungal pathogen notorious for persistent skin colonization and transmission in healthcare settings. Here, Zhao et al. explore the mechanisms driving pathogen’s adherence to skin, involving a conserved adhesin, as well as the potential of collagen coatings as a strategy to reduce C. auris adherence to abiotic surfaces.

  PublisherOA PDFDOI

• <i>Candida auris</i> skin colonization is mediated by Als4112 and interactions with host extracellular matrix proteins

  bioRxiv (Cold Spring Harbor Laboratory) · 2025-02-13 · 3 citations

  preprintOpen access

  Abstract Candida auris is an often multidrug-resistant fungal pathogen notorious for persistent skin colonization and transmission in healthcare settings. However, the mechanisms driving its adherence to skin remain poorly understood. Here, we developed in vitro systems to allow for detailed analysis of early skin colonization events and identified critical host and pathogen mediators of attachment. Across multiple strains and clades of C. auris, we identified that Als4112, a conserved adhesin, is required for skin colonization via keratinocyte attachment and direct interactions with host extracellular matrix (ECM) proteins, especially basement membrane proteins such as laminin. In a murine epicutaneous infection and human skin explants, deletion of ALS4112 significantly reduced skin colonization, underscoring its essential role in establishing cutaneous persistence. Als4112 also contributes to systemic infection, highlighting the connection between adherence and pathogenicity in this organism. Finally, coating plastic and catheter surfaces with collagen I or III markedly inhibited C. auris attachment and biofilm formation, offering an approach to curb nosocomial transmission. Our study highlights the critical role of Als4112 in C. auris colonization and virulence in vivo , making it an attractive target for future vaccine development. This study also explores the potential of specific collagen coatings as a novel strategy to prevent C. auris adherence to abiotic surfaces, offering new therapeutic avenues to control the spread of C. auris in healthcare settings.

  PublisherOA PDFDOI

Recent grants

• Characterizing Candida auris skin colonization and high-burden biofilm formation

  NIH · $427k · 2021–2025

• Mechanism(s) of pathogenicity for Candida auris

  NIH · $2.7M · 2020–2027

• NIH Grant K08AI108727

  NIH · $1.2M · 2020

Frequent coauthors

• David R. Andes

  University of Wisconsin–Madison

  81 shared

• Chad Johnson

  University of Wisconsin–Madison

  27 shared

• John F. Kernien

  University of Wisconsin–Madison

  17 shared

• Robert Żarnowski

  University of Wisconsin–Madison

  16 shared

• Hiram Sánchez

  University of Wisconsin–Madison

  16 shared

• Aaron P. Mitchell

  University of Georgia

  15 shared

• Karen Marchillo

  14 shared

• Scott G. Filler

  University of California, Los Angeles

  13 shared

Labs

• Nett ResearchPI

Education

• B.S.

  University of Wisconsin

  1999

• M.D.

  University of Wisconsin

  2003

• Ph.D.

  University of Wisconsin

  2009

Awards & honors

• 2013, Burroughs Wellcome Fund Career Award for Medical Scien…
• 2013, UW-Madison Dickie Research Award