About

Natalie Boyle is an Assistant Research Professor in the Department of Entomology at Pennsylvania State University. Her areas of expertise include honey bees, managed solitary bees, crop pollination, pollinator ecology, and integrated pest and pollinator management. She is involved in research related to pollinator health, behavior, and management strategies to enhance agricultural productivity and pollinator conservation. Her work focuses on understanding the nutritional, foraging, and nesting preferences of solitary bees, as well as the effects of environmental stressors such as heat exposure on bee sperm quality. Boyle's research also explores the role of wildflower plantings in promoting bee reproduction and the dynamics of pollination services in agricultural systems. She contributes to the Center for Pollinator Research and the Insect Biodiversity Center, advancing knowledge on pollinator biodiversity and sustainable management practices.

Research topics

• Biology
• Biochemistry
• Chemistry
• Virology
• Artificial Intelligence
• Computer Science
• Molecular biology
• Computational biology
• Medicine
• Cell biology
• Physics
• Computational chemistry
• Pharmacology
• Biophysics

Selected publications

• Systemic rhythmicity of host and bacterial bile acid amidates in the mouse

  Cell Systems · 2026-03-26 · 1 citations

  articleOpen access
  PublisherOA PDFDOI

• Glucuronidation metabolomic fingerprinting to map host-microbe metabolism

  Nature Communications · 2026-05-20

  articleOpen access1st authorCorresponding

  Glucuronidation is an important detoxification pathway that operates in balance with gastrointestinal microbial β-glucuronidase (GUS) activity, which can regenerate bioactive metabolites from their glucuronidated forms. How this host-microbe interaction shapes the distribution and pool of glucuronidated metabolites (i.e., the glucuronidome) remains poorly understood. In this study, we employed pattern-filtering data science approaches in conjunction with untargeted LC-MS/MS metabolomics to map the glucuronidome in urine, serum, and colon/fecal samples from gnotobiotic and conventional mice, and in humans. We find that microbial colonization and GUS activity compress the colonic glucuronidome and expand urinary glucuronidome diversity, revealing a compartmental redistribution of glucuronidated metabolites. Reverse metabolomics of known glucuronidated chemicals and glucuronidation pattern filtering searches in public metabolomics datasets exposed the diversity of glucuronidated metabolites in human and mouse ecosystems. In summary, we present a glucuronidation fingerprint resource that provides broader access to and analysis of the glucuronidome. Together, this work establishes a scalable analytical framework and provides mechanistic insight into how microbial activity reshapes systemic glucuronidation, with implications for drug metabolism, diet-microbe interactions, and biomarker discovery.

  PublisherOA PDFDOI

• Glucuronidation Metabolomic Fingerprinting to Map Host-Microbe Metabolism

  Research Square · 2025-04-08 · 2 citations

  preprintOpen access
  PublisherOA PDFDOI

• Gut microbiota impact on drug metabolism, bioavailability, and biotransformation

  Elsevier eBooks · 2025-12-05

  book-chapter1st authorCorresponding
  PublisherDOI

• Contributors

  Elsevier eBooks · 2025-12-05

  book-chapter
  PublisherDOI

• Systemic Rhythmicity of Host and Bacterial Bile Acid Amidates Across the Mammalian Body

  SSRN Electronic Journal · 2025-01-01

  preprintOpen access
  PublisherDOI

• Inactivation of HCoV-NL63 and SARS-CoV-2 in aqueous solution by 254 nm UV-C

  Journal of Photochemistry and Photobiology B Biology · 2023-07-05 · 5 citations

  article
  PublisherDOI

• Aryl hydrocarbon receptor activation affects nitrergic neuronal survival and delays intestinal motility in mice

  Toxicological Sciences · 2023-02-11 · 6 citations

  articleOpen access

  Despite progress describing the effects of persistent organic pollutants (POPs) on the central nervous system, the effect of POPs on enteric nervous system (ENS) function remains underexplored. We studied the effects of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), a POP, and a potent aryl hydrocarbon receptor (AHR) ligand, on the ENS and intestinal motility in mice. C57Bl/6J mice treated with TCDD (2.4 µg/kg body weight) for 8 weeks (once per week) exhibited significant delay in intestinal motility as shown by reduced stool frequency, prolonged intestinal transit time, and a persistence of dye in the jejunum compared to control mice with maximal dye retention in the ileum. TCDD significantly increased Cyp1a1 expression, an AHR target gene, and reduced the total number of neurons and affected nitrergic neurons in cells isolated from WT mice, but not Ahr-/- mice. In immortalized fetal enteric neuronal cells, TCDD-induced nuclear translocation of AHR as well as increased Cyp1a1 expression. AHR activation did not affect neuronal proliferation. However, AHR activation resulted in enteric neuronal toxicity, specifically, nitrergic neurons. Our results demonstrate that TCDD adversely affects nitrergic neurons and thereby contributes to delayed intestinal motility. These findings suggest that AHR signaling in the ENS may play a role in modulating TCDD-induced gastrointestinal pathophysiology.

  PublisherOA PDFDOI

• Neutralizing Aptamers Block S/RBD‐ACE2 Interactions and Prevent Host Cell Infection

  Angewandte Chemie · 2021-03-08 · 30 citations

  articleOpen access

  Abstract The receptor‐binding domain (RBD) of the severe acute respiratory syndrome coronavirus 2 spike (S) protein plays a central role in mediating the first step of virus infection to cause disease: virus binding to angiotensin‐converting enzyme 2 (ACE2) receptors on human host cells. Therefore, S/RBD is an ideal target for blocking and neutralization therapies to prevent and treat coronavirus disease 2019 (COVID‐19). Using a target‐based selection approach, we developed oligonucleotide aptamers containing a conserved sequence motif that specifically targets S/RBD. Synthetic aptamers had high binding affinity for S/RBD‐coated virus mimics ( K D ≈7 nM) and also blocked interaction of S/RBD with ACE2 receptors (IC 50 ≈5 nM). Importantly, aptamers were able to neutralize S protein‐expressing viral particles and prevent host cell infection, suggesting a promising COVID‐19 therapy strategy.

  PublisherOA PDFDOI

• Computational prediction of the effect of amino acid changes on the binding affinity between SARS-CoV-2 spike protein and the human ACE2 receptor

  bioRxiv (Cold Spring Harbor Laboratory) · 2021-03-25 · 5 citations

  preprintOpen access

  ABSTRACT The association of the receptor binding domain (RBD) of SARS-CoV-2 viral spike with human angiotensin converting enzyme (hACE2) represents the first required step for viral entry. Amino acid changes in the RBD have been implicated with increased infectivity and potential for immune evasion. Reliably predicting the effect of amino acid changes in the ability of the RBD to interact more strongly with the hACE2 receptor can help assess the public health implications and the potential for spillover and adaptation into other animals. Here, we introduce a two-step framework that first relies on 48 independent 4-ns molecular dynamics (MD) trajectories of RBD-hACE2 variants to collect binding energy terms decomposed into Coulombic, covalent, van der Waals, lipophilic, generalized Born electrostatic solvation, hydrogen-bonding, π-π packing and self-contact correction terms. The second step implements a neural network to classify and quantitatively predict binding affinity using the decomposed energy terms as descriptors. The computational base achieves an accuracy of 82.2% in terms of correctly classifying single amino-acid substitution variants of the RBD as worsening or improving binding affinity for hACE2 and a correlation coefficient r of 0.69 between predicted and experimentally calculated binding affinities. Both metrics are calculated using a 5-fold cross validation test. Our method thus sets up a framework for effectively screening binding affinity change with unknown single and multiple amino-acid changes. This can be a very valuable tool to predict host adaptation and zoonotic spillover of current and future SARS-CoV-2 variants.

  PublisherOA PDFDOI

Frequent coauthors

• Suresh V. Kuchipudi

  University of Pittsburgh

  8 shared

• Victoria S. Cavener

  Pennsylvania State University

  6 shared

• Ruth H. Nissly

  Pennsylvania State University

  4 shared

• Meera Surendran Nair

  4 shared

• Edurne Rujas

  Biofisika

  3 shared

• Abhinay Gontu

  Pennsylvania State University

  3 shared

• Xinping Fu

  2 shared

• Costas D. Maranas

  Pennsylvania State University

  2 shared

Labs

• Boyle LabPI

Education

• Doctorate of Philosophy , Integrated and Biomedical Physiology

  The Pennsylvania State University

• Master of Public Health

  New York Medical College

  2019