Lauren Bird on Muck Rack

Lauren Bird

As seen in: MSN, MSN Canada, MSN Money Canada, Nature, Yahoo News, Canadian Broadcasting Corporation (CBC), CBAP-FM (Shelburne, NS), CBAT-TV (Fredericton, NB), CBC New Brunswick, CBC News and
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Articles

Conformational dynamics, RNA binding, and phase separation regulate the multifunctionality of rabies virus P protein - Nature Communications

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By Stephen Rawlinson, Shatabdi Chakraborty, Ashish Sethi, Lauren Bird, Tianyue Zhao, David Jans, Nicholas Williamson, Senthil Arumugam, Paul Gooley
| Nature
Abstract RNA viruses encode multifunctional proteins to overcome limited genomic capacity and mediate diverse processes in viral replication and host cell modulation. The rabies virus P gene encodes full-length P1 protein and the truncated isoform, P3, which acquires phenotypes absent from P1, including interactions with cellular membrane-less organelles (MLOs) formed by liquid-liquid phase separation (LLPS).
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Intralysosomal pathogens differentially influence the proteolytic potential of their niche

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By Lauren Bird, Bangyan Xu, Patrice Newton, Nichollas E Scott
| biorxiv.org
Abstract Avoiding lysosomal degradation is vital to the success of intracellular pathogens. The Gram-negative bacterium Coxiella burnetii and protozoan parasites of the Leishmania genus are unique in being able to replicate within the mature phagolysosomal compartment of host cells, though the exact mechanisms utilised to withstand this hostile environment are not clearly defined. We recently reported that C. burnetii removes the lysosomal protease cathepsin B during infection of mammalian cells.
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Coxiella burnetii manipulates the lysosomal protease cathepsin B to facilitate intracellular success - Nature Communications

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By Lauren Bird, Bangyan Xu, Andrew Hobbs, Alexander Ziegler, Nichollas E Scott, Patrice Newton, David Thomas, Laura E Edgington-Mitchell
| Nature
Abstract The obligate intracellular bacterium Coxiella burnetii establishes an intracellular replicative niche termed the Coxiella-containing vacuole (CCV), which has been characterised as a bacterially modified phagolysosome. How C. burnetii withstands the acidic and degradative properties of this compartment is not well understood. We demonstrate that the key lysosomal protease cathepsin B is actively and selectively removed from C.
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