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Reposted by Lauren Bird

Becky Lamason @lamasonlab.bsky.social · 24/02/2026

Excited to share our latest work from first author Patrick Woida. Using a novel surface display platform for expression of split TurboID, we discovered that CYLD is recruited to the Listeria surface via the effector InlC and that it supports cell-to-cell spread www.biorxiv.org/content/10.6...

biorxiv.org

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Reposted by Lauren Bird

Becky Lamason @lamasonlab.bsky.social · 06/01/2026

Check out our latest paper from first author Allison Scott using a powerful enrichment strategy to enable transcriptional profiling of the early stages of a rickettsial infection

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Reposted by Lauren Bird

Becky Lamason @lamasonlab.bsky.social · 29/10/2025

Thrilled to share our latest story from postdoc @sitbrandon.bsky.social! Using a functional genetic screen, he discovered an unexpected way that Rickettsia relies on the host to stabilize the Sca2 surface protein that drives pathogen motility and virulence.

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Reposted by Lauren Bird

PLOS Biology @plosbiology.org · 25/07/2025

#Legionella pumps 100s of effector proteins into host cells, including to #mitochondria. @drdstojanovski.bsky.social &co show that effector LpPIP is a tail-anchored protein of the MOM that recruits protein phosphatase 1 to modulate the host mitochondrial P-proteome @plosbiology.org 🧪 plos.io/4f2T5kE

Top: HeLa cells expressing FLAGLpPIP, or FLAGRVxFdead were stained with 100 nM MitoTracker Deep Red FM (mitochondria; MTDR) and, following fixation, processed for immunofluorescence using antibodies against FLAG (green) and PPP1CB (magenta). Nuclei were stained with Hoechst 33258 (blue). Scale bar represents 10 μm. Fluorescence signal profiles of FLAG and PPP1CB were measured across the indicated line of interest. Bottom: AlphaFold3 structure of LpPIP-PPP1CB complex labeled with the active site (purple) and three substrate binding grooves (yellow) of PPP1CB.

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Lauren Bird @laurenbird.bsky.social · 25/04/2025

Excited to share this story from my PhD, out today in Nature Communications! We show that Coxiella removes cathepsin B to reduce lysosomal hostility and promote bacterial success. This depends on a vacuole established by effector CvpB. www.nature.com/articles/s41...

nature.com

Coxiella burnetii manipulates the lysosomal protease cathepsin B to facilitate intracellular success - Nature Communications

The zoonotic pathogen Coxiella burnetiiestablishes a unique intracellular niche within a lysosome-derived vacuole. Here Bird et al. undertook proteomic, cell biology and microbiology approaches to cha...

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