Honors & Awards

  • Gabilan Stanford Graduate Fellowship in Science and Engineering, Stanford University (2012-2015)
  • Lubert Stryer Bio-X Stanford Interdisciplinary Graduate Fellowship, Stanford University (2015-2018)

Education & Certifications

  • Master of Science, Utrecht University, Infectious Diseases and Immunology (2011)
  • Bachelor of Science, Utrecht University, Pre-Med (2009)

Stanford Advisors

Service, Volunteer and Community Work

  • Volunteer, Maitland Cottage Home (July 1, 2008 - July 31, 2008)

    Assisted in surgeries and daily care of pediatric orthopedic patients in a hospital in Cape Town, South Africa.


    Maitland Cottage Home, Cape Town

  • Volunteer, Science is Elementary (4/1/2013)

    Teach STEM classes to elementary school students in the Bay Area.


    Bay Area, California, USA


Work Experience

  • Research Assistant, Stanford University (March 1, 2012)


    VA Palo Alto Health Care System

  • Research Trainee, Brigham and Women's Hospital, Harvard Medical School (February 14, 2011 - February 29, 2012)


    Brigham and Women's Hospital


All Publications

  • Modified High-Molecular-Weight Hyaluronan Promotes Allergen-Specific Immune Tolerance AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY Gebe, J. A., Yadava, K., Ruppert, S. M., Marshall, P., Hill, P., Falk, B. A., Sweere, J. M., Han, H., Kaber, G., Medina, C., Mikecz, K., Ziegler, S. F., Balaji, S., Keswani, S. G., Perez, V. A., Butte, M. J., Nadeau, K., Altemeier, W. A., Fanger, N., Bollyky, P. L. 2017; 56 (1): 109-120


    The extracellular matrix in asthmatic lungs contains abundant low-molecular-weight hyaluronan, and this is known to promote antigen presentation and allergic responses. Conversely, high-molecular-weight hyaluronan (HMW-HA), typical of uninflamed tissues, is known to suppress inflammation. We investigated whether HMW-HA can be adapted to promote tolerance to airway allergens. HMW-HA was thiolated to prevent its catabolism and was tethered to allergens via thiol linkages. This platform, which we call "XHA," delivers antigenic payloads in the context of antiinflammatory costimulation. Allergen/XHA was administered intranasally to mice that had been sensitized previously to these allergens. XHA prevents allergic airway inflammation in mice sensitized previously to either ovalbumin or cockroach proteins. Allergen/XHA treatment reduced inflammatory cell counts, airway hyperresponsiveness, allergen-specific IgE, and T helper type 2 cell cytokine production in comparison with allergen alone. These effects were allergen specific and IL-10 dependent. They were durable for weeks after the last challenge, providing a substantial advantage over the current desensitization protocols. Mechanistically, XHA promoted CD44-dependent inhibition of nuclear factor-κB signaling, diminished dendritic cell maturation, and reduced the induction of allergen-specific CD4 T-helper responses. XHA and other potential strategies that target CD44 are promising alternatives for the treatment of asthma and allergic sinusitis.

    View details for DOI 10.1165/rcmb.2016-0111OC

    View details for Web of Science ID 000392133000012

    View details for PubMedCentralID PMC5248962

  • Pf4 bacteriophage produced by Pseudomonas aeruginosa inhibits Aspergillus fumigatus metabolism via iron sequestration MICROBIOLOGY-SGM Penner, J. C., Ferreira, J. A., Secor, P. R., Sweere, J. M., Birukova, M. K., Joubert, L., Haagensen, J. A., Garcia, O., Malkovskiy, A. V., Kaber, G., Nazik, H., Manasherob, R., Spormann, A. M., Clemons, K. V., Stevens, D. A., Bollyky, P. L. 2016; 162 (9): 1583-1594


    Pseudomonas aeruginosa (Pa) and Aspergillus fumigatus (Af) are major human pathogens known to interact in a variety of disease settings, including airway infections in cystic fibrosis. We recently reported that clinical CF isolates of Pa inhibit the formation and growth of Af biofilms. Here, we report that the bacteriophage Pf4, produced by Pa, can inhibit the metabolic activity of Af biofilms. This phage-mediated inhibition was dose dependent, ablated by phage denaturation, and was more pronounced against preformed Af biofilm rather than biofilm formation. In contrast, planktonic conidial growth was unaffected. Two other phages, Pf1 and fd, did not inhibit Af, nor did supernatant from a Pa strain incapable of producing Pf4. Pf4, but not Pf1, attaches to Af hyphae in an avid and prolonged manner, suggesting that Pf4-mediated inhibition of Af may occur at the biofilm surface. We show that Pf4 binds iron, thus denying Af a crucial resource. Consistent with this, the inhibition of Af metabolism by Pf4 could be overcome with supplemental ferric iron, with preformed biofilm more resistant to reversal. To our knowledge, this is the first report of a bacterium producing a phage that inhibits the growth of a fungus and the first description of a phage behaving as an iron chelator in a biological system.

    View details for DOI 10.1099/mic.0.000344

    View details for Web of Science ID 000385273100008

    View details for PubMedID 27473221

  • Filamentous Bacteriophage Promote Biofilm Assembly and Function CELL HOST & MICROBE Secor, P. R., Sweere, J. M., Michaels, L. A., Malkovskiy, A. V., Lazzareschi, D., Katznelson, E., Rajadas, J., Birnbaum, M. E., Arrigoni, A., Braun, K. R., Evanko, S. P., Stevens, D. A., Kaminsky, W., Singh, P. K., Parks, W. C., Bollyky, P. L. 2015; 18 (5): 549-559


    Biofilms-communities of bacteria encased in a polymer-rich matrix-confer bacteria with the ability to persist in pathologic host contexts, such as the cystic fibrosis (CF) airways. How bacteria assemble polymers into biofilms is largely unknown. We find that the extracellular matrix produced by Pseudomonas aeruginosa self-assembles into a liquid crystal through entropic interactions between polymers and filamentous Pf bacteriophages, which are long, negatively charged filaments. This liquid crystalline structure enhances biofilm function by increasing adhesion and tolerance to desiccation and antibiotics. Pf bacteriophages are prevalent among P. aeruginosa clinical isolates and were detected in CF sputum. The addition of Pf bacteriophage to sputum polymers or serum was sufficient to drive their rapid assembly into viscous liquid crystals. Fd, a related bacteriophage of Escherichia coli, has similar biofilm-building capabilities. Targeting filamentous bacteriophage or the liquid crystalline organization of the biofilm matrix may represent antibacterial strategies.

    View details for DOI 10.1016/j.chom.2015.10.013

    View details for Web of Science ID 000365113100008

    View details for PubMedID 26567508

    View details for PubMedCentralID PMC4653043

  • Orphan chemoattractant receptor GPR15 mediates dendritic epidermal T-cell recruitment to the skin EUROPEAN JOURNAL OF IMMUNOLOGY Lahl, K., Sweere, J., Pan, J., Butcher, E. 2014; 44 (9): 2577-2581
  • Autochthonous and dormant Cryptococcus gattii infections in Europe. Emerging infectious diseases Hagen, F., Colom, M. F., Swinne, D., Tintelnot, K., Iatta, R., Montagna, M. T., Torres-Rodriguez, J. M., Cogliati, M., Velegraki, A., Burggraaf, A., Kamermans, A., Sweere, J. M., Meis, J. F., Klaassen, C. H., Boekhout, T. 2012; 18 (10): 1618-1624


    Until recently, Cryptococcus gattii infections occurred mainly in tropical and subtropical climate zones. However, during the past decade, C. gattii infections in humans and animals in Europe have increased. To determine whether the infections in Europe were acquired from an autochthonous source or associated with travel, we used multilocus sequence typing to compare 100 isolates from Europe (57 from 40 human patients, 22 from the environment, and 21 from animals) with 191 isolates from around the world. Of the 57 human patient isolates, 47 (83%) were obtained since 1995. Among the 40 patients, 24 (60%) probably acquired the C. gattii infection outside Europe; the remaining 16 (40%) probably acquired the infection within Europe. Human patient isolates from Mediterranean Europe clustered into a distinct genotype with animal and environmental isolates. These results indicate that reactivation of dormant C. gattii infections can occur many years after the infectious agent was acquired elsewhere.

    View details for DOI 10.3201/eid1810.120068

    View details for PubMedID 23017442

    View details for PubMedCentralID PMC3471617

  • Defect in regulatory B-cell function and development of systemic autoimmunity in T-cell Ig mucin 1 (Tim-1) mucin domain-mutant mice PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Xiao, S., Brooks, C. R., Zhu, C., Wu, C., Sweere, J. M., Petecka, S., Yeste, A., Quintana, F. J., Ichimura, T., Sobel, R. A., Bonventre, J. V., Kuchroo, V. K. 2012; 109 (30): 12105-12110


    Tim-1, a type I transmembrane glycoprotein, consists of an IgV domain and a mucin domain. The IgV domain is essential for binding Tim-1 to its ligands, but little is known about the role of the mucin domain, even though genetic association of TIM-1 with atopy/asthma has been linked to the length of mucin domain. We generated a Tim-1-mutant mouse (Tim-1(Δmucin)) in which the mucin domain was deleted genetically. The mutant mice showed a profound defect in IL-10 production from regulatory B cells (Bregs). Associated with the loss of IL-10 production in B cells, older Tim-1(Δmucin) mice developed spontaneous autoimmunity associated with hyperactive T cells, with increased production of IFN-γ and elevated serum levels of Ig and autoantibodies. However, Tim-1(Δmucin) mice did not develop frank systemic autoimmune disease unless they were crossed onto the Fas-mutant lpr mice on a C57BL/6 background. Tim-1(Δmucin)lpr mice developed accelerated and fulminant systemic autoimmunity with accumulation of abnormal double-negative T cells and autoantibodies to a number of lupus-associated autoantigens. Thus, Tim-1 plays a critical role in maintaining suppressive Breg function, and our data also demonstrate an unexpected role of the Tim-1 mucin domain in regulating Breg function and maintaining self-tolerance.

    View details for DOI 10.1073/pnas.1120914109

    View details for Web of Science ID 000306992700050

    View details for PubMedID 22773818

    View details for PubMedCentralID PMC3409739