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Biology subjects

Adan, W. C.

Publications and source records attributed to Adan, W. C..

2 recordsLinked to original sources

ppigFinder: an integrated desktop application for bacterial genome annotation and AlphaFold 3 based protein protein interaction screening

Motivation. AlphaFold-based structure prediction has transformed structural biology by enabling accurate protein modelling and providing a powerful framework for inferring protein-protein interactions (PPIs). However, discovering candidate PPIs directly from genome sequences remains a fragmented and largely trial-and-error process, typically requiring separate tools for open reading frame (ORF) prediction, functional annotation, candidate selection, iterative testing of potential partners, manual preparation of individual structural-prediction jobs, and downstream interpretation of confidence metrics. Results. We present Protein-Protein Interaction Genomic Finder (ppigFinder), a standalone, cross-platform desktop application that integrates these steps into a project-oriented graphical workflow for genome-based PPI discovery from nucleotide sequence data. ppigFinder combines ORF prediction, functional annotation, genomic-neighbourhood inspection, AlphaFold 3 job generation, remote job submission, and structural-confidence analysis within a single environment. As a proof of concept, we performed a VirD4-centered AlphaFold 3 interactome screen in Xanthomonas citri pv. citri strain 306, modelling VirD4 (ORF2601) against all 4,303 predicted chromosomal ORFs. Ranking by the minimum interchain predicted aligned error (PAE_min) placed all 14 XVIPCD-containing effector candidates within the top 1% of predictions, with the six top-ranked models corresponding to XVIP candidates. The screen also recovered an XVIPCD-containing protein absent from the reference genome annotation and identified high-confidence candidates predicted to bind VirD4 at a surface opposite to the XVIPCD-binding site.

bioinformatics↗

To Kill or not to Kill: A Conserved trans-intoxication protection factor Blocks X-T4SS-Mediated Fratricide through Interaction with VirB5

Bacteria can outcompete rivals by using specialized secretion systems to deliver toxic effectors into prey cells. How these systems distinguish prey from kin remains a fundamental unanswered question. In many Xanthomonadales (Lysobacterales) species, the antibacterial type IV secretion system (X-T4SS) mediates cell-cell contact-dependent killing of competing bacteria. Here, we identified XAC2611, a chromosomally encoded, cysteine-rich DUF4189 protein, as essential for preventing X-T4SS-mediated fratricide among sibling cells in Xanthomonas citri. XAC2611 homologs are found within or proximal to the genomic loci coding almost all identified X-T4SS. Live-cell microscopy and biochemical data reveal that XAC2611 is abundantly produced and widely distributed throughout the periplasm of recipient cells and is required to prevent X. citri cells from intoxicating each other in a contact-dependent manner. We also show that XAC2611 homologs from Stenotrophomonas maltophilia protect X. citri cells from attack by S. maltophilia. Protein-protein interaction assays show that XAC2611 interacts directly with the VirB5 subunit. Since VirB5 is predicted to be localized at the tip of the X-T4SS pilus, its interaction with XAC2611 in a neighboring sister cell could block X-T4SS-mediated effector delivery. We therefore name this family of proteins trans-intoxication protection factors (Tpfs).

microbiology↗