>:P
A good way store scholarly work is through a DOI. Story short, a DOI is a persistent identifier for a piece of work as string or URL. The purpose of a persistent identifier means should the author(s) change the location of the work online—like a different website, page, or journal—the DOI will still point to the work.
Sharing DOIs builds intellectual rigor and trust by supporting formatting consistency while being a popular way of sharing work in academia.
Writing a paper that means a lot to you and want it to be free to view anywhere? Place it into an online research repository. These repositories act to enhance a work's engagement by creating a unique DOI to your work and allows for easy sharing. For example, Zenodo is owned by the particle physics giant, CERN, and continues to be an honorable research repository. Harvard owns one and so do many other organizations, universities and institutions alike.
Some pointers:
[1] zenodo.org
[2] rd-alliance.org/wp-content/uploads/2024/03/Generalist20Repository20Comparison20Chart-2.pdf
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
XM1 Subunit
Shown above is a protein subunit. A subunit, as the name implies, is part of a bigger, more larger structure like a virus (see left). Because it's part of a more large-scale structure, a subunit usually has special properties like self-assembly, allowing for the formation of said large structure.
By creating many copies of this single XM1 phage subunit by the bacteria species Vibrio—a bacteria known to cause gastroenteritis through contaminated food or water—the virally infected, and now reprogrammed bacteria produces 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, again. 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 in allowing better recovery efforts.
Hi, I'm David!
I'm a web developer, research hobbyist, and medical lab assistant.
In the meantime, I write manuscripts and papers to analyze structural biology research. I try to make concepts easy for those new to protein science and hope to cover knowledge gaps and keep up with the latest trends. Story short, I'm a proud nerd.
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