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Your search keyword '"Gruenheid, Samantha"' showing total 17 results
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17 results on '"Gruenheid, Samantha"'

5. Modeling gene-environment interactions in Parkinson's Disease: Helicobacter pylori infection of Pink1-/- mice induces CD8 T cell-dependent motor and cognitive dysfunction.

Author

Kazanova, Alexandra, primary, Sung, Jacqueline, additional, Oliveira, Nathalia Luisa, additional, Gavino, Christina, additional, Bessaiah, Hicham, additional, Pei, Jessica, additional, Burns, Lindsay, additional, Miller, Willemein, additional, Brouillard-Galipeau, Morgane, additional, Zhu, Lei, additional, Guerra, Lucia Marguerite, additional, Elemeery, Moustafa Nouh, additional, Recinto, Sherilyn Junelle, additional, MacDonald, Adam, additional, Lanoix, Joel, additional, Thibault, Pierre, additional, McBride, Heidi M., additional, Desjardins, Michel, additional, Stratton, Jo Anne, additional, Labrecque, Nathalie, additional, and Gruenheid, Samantha, additional

Published
2024
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7. LRRK2 regulates the activation of the unfolded protein response and antigen presentation in macrophages during inflammation

Author

Fahmy, Ahmed M., primary, Cannon, Tyler, additional, Paredes, Camberly Herdandez, additional, Ahmadi, Ali, additional, Xu, Yong Zhong, additional, Barette, Benoit, additional, Ibrahim, Maha, additional, Lanoix, Joël, additional, Arango-Duque, Guillermo, additional, Schurr, Erwin, additional, Chevet, Eric, additional, Thibault, Pierre, additional, Gruenheid, Samantha, additional, McBride, Heidi, additional, and Desjardins, Michel, additional

Published
2023
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12. The bacterial virulence factor NleA undergoes host‐mediated O‐linked glycosylation.

Author

Burns, Lindsay, Giannakopoulou, Natalia, Zhu, Lei, Xu, Yong Zhong, Khan, Rufaida H., Bekal, Sadjia, Schurr, Erwin, Schmeing, T. Martin, and Gruenheid, Samantha

Subjects
GLYCOSYLATION, MIXED infections, BACTERIAL proteins, HOSTS (Biology), CYTOLOGY
Abstract

Enterohaemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC) are gastrointestinal pathogens responsible for severe diarrheal illness. EHEC and EPEC form "attaching and effacing" lesions during colonization and, upon adherence, inject proteins directly into host intestinal cells via the type III secretion system (T3SS). Injected bacterial proteins have a variety of functions but generally alter host cell biology to favor survival and/or replication of the pathogen. Non‐LEE‐encoded effector A (NleA) is a T3SS‐injected effector of EHEC, EPEC, and the related mouse pathogen Citrobacter rodentium. Studies in mouse models indicate that NleA has an important role in bacterial virulence. However, the mechanism by which NleA contributes to disease remains unknown. We have determined that the following translocation into host cells, a serine and threonine‐rich region of NleA is modified by host‐mediated mucin‐type O‐linked glycosylation. Surprisingly, this region was not present in several clinical EHEC isolates. When expressed in C. rodentium, a non‐modifiable variant of NleA was indistinguishable from wildtype NleA in an acute mortality model but conferred a modest increase in persistence over the course of infection in mixed infections in C57BL/6J mice. This is the first known example of a bacterial effector being modified by host‐mediated O‐linked glycosylation. Our data also suggests that this modification may confer a selective disadvantage to the bacteria during in vivo infection. [ABSTRACT FROM AUTHOR]

Published
2023
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14. RpoN-Based stapled peptides with improved DNA binding suppress Pseudomonas aeruginosa virulence

Author

Paquette, André R., primary, Payne, Sterling R., additional, McKay, Geoffrey A., additional, Brazeau-Henrie, Jordan T., additional, Darnowski, Micheal G., additional, Kammili, Anitha, additional, Bernal, Federico, additional, Mah, Thien-Fah, additional, Gruenheid, Samantha, additional, Nguyen, Dao, additional, and Boddy, Christopher N., additional

Published
2022
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17. RpoN-Based stapled peptides with improved DNA binding suppress Pseudomonas aeruginosavirulenceElectronic supplementary information (ESI) available. See DOI: 10.1039/d1md00371b

Author

Paquette, André R., Payne, Sterling R., McKay, Geoffrey A., Brazeau-Henrie, Jordan T., Darnowski, Micheal G., Kammili, Anitha, Bernal, Federico, Mah, Thien-Fah, Gruenheid, Samantha, Nguyen, Dao, and Boddy, Christopher N.

Abstract

Stapled peptides have the ability to mimic α-helices involved in protein binding and have proved to be effective pharmacological agents for disrupting protein–protein interactions. DNA-binding proteins such as transcription factors bind their cognate DNA sequences viaan α-helix interacting with the major groove of DNA. We previously developed a stapled peptide based on the bacterial alternative sigma factor RpoN capable of binding the RpoN DNA promoter sequence and inhibiting RpoN-mediated expression in Escherichia coli. We have elucidated a structure–activity relationship for DNA binding by this stapled peptide, improving DNA binding affinity constants in the high nM range. Lead peptides were shown to have low toxicity as determined by their low hemolytic activity at 100 μM and were shown to have anti-virulence activity in a Galleria mellonellamodel of Pseudomonas aeruginosainfection. These findings support further preclinical development of stapled peptides as antivirulence agents targeting P. aeruginosa.

Published
2022
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