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Sohini Deb

@sohini-d.bsky.social
28 followers 51 following 1 posts

Assistant Professor at University of Copenhagen| Plant molecular biologist | Exploring lipid biology and effector interactions in plant-fungal pathogens 🌾🌿

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Reposted by Sohini Deb
New Phytologist @newphyt.bsky.social · 21/03/2026
#TansleyInsight: Entanglement of plant immunity and endomembrane trafficking revealed by plant–powdery mildew fungal interactions Thordal-Christensen et al. 👇 📖 nph.onlinelibrary.wiley.com/doi/10.1111/... #LatestIssue #PlantScience @sohini-d.bsky.social
Fig. 2 Model for membrane trafficking in the immune response to powdery mildew fungi.
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Sohini Deb @sohini-d.bsky.social · 07/03/2026
Happy to have contributed to this 🎉
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Reposted by Sohini Deb
Journal of Experimental Botany @jxbotany.bsky.social · 25/11/2025
🛡️ INSIGHT 🛡️ "Barley powdery mildew effector CSEP0162 interacts with the endosome membrane-binding domain of barley MON1" - Deb et al. share an update relevant to their earlier work, Liao et al. (2022) 🌾 Insight 🔗 doi.org/10.1093/jxb/... Research 🔗 doi.org/10.1093/jxb/... #PlantScience 🧪
Fig. 1 (shortened, full legend in paper): CSEP0162 interacts with the C-terminus, but not ‘full-length’ HvMON1 in Y2H. The yeast strain Y8930 was transformed with constructs fusing either CSEP0162, CSEP0105, or HvCCZ1 with the GAL4 DNA-binding-domain (BD) (pDEST-AS2-1 vector, cloned from respective pENTR clones using Gateway LR cloning). The yeast strain Y8800 was transformed with either empty vector pDEST-ACT2, or constructs fusing either amino acids 22–598 of HvMON1 or the C-terminus (amino acids 539–598) of HvMON1 with the activation domain (AD) (pDEST-ACT2 vector, cloned from the respective pENTR clones using Gateway LR cloning). Transformed strains were mated in the listed combinations and plated on dropout (DO) medium lacking leucine (L) and tryptophan (W). Drop test was performed by adjusting cultures to OD600 = 1.0 (100), and with further serial dilutions (10–1 and 10–2). Growth on these plates indicates the presence of both constructs.
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