Publications by authors named "Melissa Mendez-Moran"
Article Synopsis
- Host-pathogen interactions are crucial for understanding infections, and while affinity-purification mass spectrometry has its uses, it has scalability and authenticity limitations.
- The study introduces co-fractionation mass spectrometry to analyze host-pathogen interactions in viral infections of two jumbophages (ϕKZ and ϕPA3) in Pseudomonas aeruginosa, detecting over 6000 interactions and providing insights into previously unknown phage proteins.
- An online platform called PhageMAP was created to make this data accessible for network querying and visualization, potentially advancing research in host-pathogen dynamics.
To protect themselves from host attack, numerous jumbo bacteriophages establish a phage nucleus-a micron-scale, proteinaceous structure encompassing the replicating phage DNA. Bacteriophage and host proteins associated with replication and transcription are concentrated inside the phage nucleus while other phage and host proteins are excluded, including CRISPR-Cas and restriction endonuclease host defense systems. Here, we show that nucleus fragments isolated from ϕPA3 infected Pseudomonas aeruginosa form a 2-dimensional lattice, having p2 or p4 symmetry.
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- Host-pathogen interactions (HPIs) are crucial for understanding how infections establish and progress; traditional methods focus on small pathogens but can be limiting.
- The researchers introduced co-fractionation mass spectrometry (SEC-MS) to analyze HPIs from two large phages, revealing over 6000 unique interactions and insights into fundamental viral mechanisms.
- To enhance accessibility, they created PhageMAP, an online tool for visualizing and querying these interactions, aimed at advancing the study of host-pathogen dynamics.