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1. Pathogen disgust sensitivity protects against infection in a high pathogen environment

   https://doi.org/10.1073/pnas.2018552118  

   Cepon-Robins, Tara J. ; Blackwell, Aaron D. ; Gildner, Theresa E. ; Liebert, Melissa A. ; Urlacher, Samuel S. ; Madimenos, Felicia C. ; Eick, Geeta N. ; Snodgrass, J. Josh ; Sugiyama, Lawrence S. ( February 2021 , Proceedings of the National Academy of Sciences)

   Disgust is hypothesized to be an evolved emotion that functions to regulate the avoidance of pathogen-related stimuli and behaviors. Individuals with higher pathogen disgust sensitivity (PDS) are predicted to be exposed to and thus infected by fewer pathogens, though no studies have tested this directly. Furthermore, PDS is hypothesized to be locally calibrated to the types of pathogens normally encountered and the fitness-related costs and benefits of infection and avoidance. Market integration (the degree of production for and consumption from market-based economies) influences the relative costs/benefits of pathogen exposure and avoidance through sanitation, hygiene, and lifestyle changes, and is thus predicted to affect PDS. Here, we examine the function of PDS in disease avoidance, its environmental calibration, and its socioecological variation by examining associations among PDS, market-related lifestyle factors, and measures of bacterial, viral, and macroparasitic infection at the individual, household, and community levels. Data were collected among 75 participants (ages 5 to 59 y) from 28 households in three Ecuadorian Shuar communities characterized by subsistence-based lifestyles and high pathogen burden, but experiencing rapid market integration. As predicted, we found strong negative associations between PDS and biomarkers of immune response to viral/bacterial infection, and weaker associations between PDS and measuresmore »of macroparasite infection, apparently mediated by market integration-related differences. We provide support for the previously untested hypothesis that PDS is negatively associated with infection, and document variation in PDS indicative of calibration to local socioeconomic conditions. More broadly, findings highlight the importance of evolved psychological mechanisms in human health outcomes.

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2. Galleria mellonella experimental model for bat fungal pathogen Pseudogymnoascus destructans and human fungal pathogen Pseudogymnoascus pannorum

   https://doi.org/10.1080/21505594.2018.1518087  

   Fuchs, Beth Burgwyn ; Chaturvedi, Sudha ; Rossoni, Rodnei Dennis ; de Barros, Patricia P. ; Torres-Velez, Fernando ; Mylonakis, Eleftherios ; Chaturvedi, Vishnu ( July 2018 , Virulence)
3. Genetic covariance in immune measures and pathogen resistance in decorated crickets is sex and pathogen specific

   https://doi.org/10.1111/1365-2656.13709  

   Letendre, Corinne ; Duffield, Kristin R. ; Sadd, Ben M. ; Sakaluk, Scott K. ; House, Clarissa M. ; Hunt, John ( April 2022 , Journal of Animal Ecology)
4. Stretching and break-up of saliva filaments during speech: A route for pathogen aerosolization and its potential mitigation

   https://doi.org/10.1103/PhysRevFluids.5.102301  

   Abkarian, M. ; Stone, H. A. ( October 2020 , Physical Review Fluids)
5. Investigating the reaction and substrate preference of indole-3-acetaldehyde dehydrogenase from the plant pathogen Pseudomonas syringae Pto DC3000

   https://doi.org/10.1042/BSR20202959  

   Zhang, Kaleena ; Lee, Josephine S. ; Liu, Regina ; Chan, Zita T. ; Dawson, Trenton J. ; De Togni, Elisa S. ; Edwards, Chris T. ; Eng, Isabel K. ; Gao, Ashley R. ; Goicouria, Luis A. ; et al ( December 2020 , Bioscience Reports)

   Abstract Aldehyde dehydrogenases (ALDHs) catalyze the conversion of various aliphatic and aromatic aldehydes into corresponding carboxylic acids. Traditionally considered as housekeeping enzymes, new biochemical roles are being identified for members of ALDH family. Recent work showed that AldA from the plant pathogen Pseudomonas syringae strain PtoDC3000 (PtoDC3000) functions as an indole-3-acetaldehyde dehydrogenase for the synthesis of indole-3-acetic acid (IAA). IAA produced by AldA allows the pathogen to suppress salicylic acid-mediated defenses in the model plant Arabidopsis thaliana. Here we present a biochemical and structural analysis of the AldA indole-3-acetaldehyde dehydrogenase from PtoDC3000. Site-directed mutants targeting the catalytic residues Cys302 and Glu267 resulted in a loss of enzymatic activity. The X-ray crystal structure of the catalytically inactive AldA C302A mutant in complex with IAA and NAD+ showed the cofactor adopting a conformation that differs from the previously reported structure of AldA. These structures suggest that NAD+ undergoes a conformational change during the AldA reaction mechanism similar to that reported for human ALDH. Site-directed mutagenesis of the IAA binding site indicates that changes in the active site surface reduces AldA activity; however, substitution of Phe169 with a tryptophan altered the substrate selectivity of the mutant to prefer octanal. The present study highlightsmore »the inherent biochemical versatility of members of the ALDH enzyme superfamily in P. syringae.« less