>:P
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A good way to find scholarly research is to find about if the paper has a DOI. Story short, a DOI is a persistent identifier for a piece of work, so that way should an author(s) change the work's location online—like a different website, journal, what have you—the original DOI will still point to the work.
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Vibrio phage XM1
Antibiotic resistance poses a growing risk to public health requiring new tools to combat pathogenic bacteria. Contractile injection systems, including bacteriophage tails, pyocins, and bacterial type VI secretion systems, can efficiently penetrate cell envelopes and become potential antibacterial agents. Bacteriophage XM1 is a dsDNA virus belonging to the Myoviridae family and infecting Vibrio bacteria. The XM1 virion, made of 18 different proteins, consists of an icosahedral head and a contractile tail, terminated with a baseplate. Here we report cryo-EM reconstructions of all components of the XM1 virion and describe atomic structures of 14 XM1 proteins. The XM1 baseplate is composed of a central hub surrounded by six wedge modules to which twelve spikes are attached. The XM1 tail contains a fewer number of smaller proteins compared with other reported phage baseplates, depicting the minimum requirements for building an effective cell-envelope-penetrating machine. We describe the tail sheath structure in the pre-infection post-infection states and its conformational changes during infection. In addition, we report, for the first time, the in situ structure of the phage neck region to near-atomic resolution. Based on these structures, we propose mechanisms of virus assembly and infection.
Abstract obtained from Wang et al., 2021 doi.org/10.3390/v15081673
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XM1 Subunit
Shown above is how this clump of proteins forms what's called a subunit. Here a subunit can have special properties like self-assembly, allowing for the formation of giant structures. Through this single, XM1 phage subunit, it can be produced readily by the cell of a species of bacteria, Vibrio, which is known to cause gastroenteritis through contaminated food or water. When the XM1 virus hijacks this illness-spreading bacteria, it'll reprogram the bacteria to produce thousands and thousands of these individual subunits, only for each piece to wiggle around in the cellular fluid until clicking together like magnets. By collectively combining with itself many of times, it forms the shell of the virus which can be shown on the left.
Keeping hopeful is that by studying this XM1 phage, it could one day be administered to those suffering from the illness to effectively arrest the disease and allowing better recovery.
Be sure to visit that paper under the image of the XM1 phage for more info.
Hi, I'm David
I'm a Medical Lab Assistant and practice writing narrative reviews for Structural Biology research. I help researchers in protein science identify critical knowledge gaps and keep up-to-date with the latest trends.
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