Malevolent Design News - How Meningococci Make Us Sick

False color scanning electron micrograph of meningococci (orange) adherent to human host cells (green).

Image credit: Alexandra Schubert-Unkmeir / Universität Würzburg

Small Protein, Big Impact - Universität Würzburg

Entering the strange world of intelligent [sic] design we find numerous examples, like Covid-19, of the sheer malevolence of any intelligence that could design such things.

Take for example, this recently discovered mechanism whereby the Meningococcal bacteria cause life-threatening meningitis and meningococcal septicaemia. It was discovered by research groups led by the Würzburg University scientists Christoph Schoen and Jörg Vogel and published in the journal Nature Communications a few days ago.

According to the Würzburg University news item:

In meningococci, the RNA-binding protein ProQ plays a major role. Together with RNA molecules, it regulates processes that are important for pathogenic properties of the bacteria.

Meningococci are bacteria that can cause life-threatening meningitis and sepsis. These pathogens use a small protein with a large impact: The RNA-binding protein ProQ is involved in the activation of more than 250 bacterial genes.

ProQ ensures that meningococci can better repair their DNA if damaged and it makes them resistant to oxidative stress. Both these factors contribute significantly to the bacteria's pathogenic properties.

This was reported by research groups led by the Würzburg scientists Christoph Schoen and Jörg Vogel in the journal Nature Communications.

Abstract
FinO-domain proteins are a widespread family of bacterial RNA-binding proteins with regulatory functions. Their target spectrum ranges from a single RNA pair, in the case of plasmid-encoded FinO, to global RNA regulons, as with enterobacterial ProQ. To assess whether the FinO domain itself is intrinsically selective or promiscuous, we determine in vivo targets of Neisseria meningitidis, which consists of solely a FinO domain. UV-CLIP-seq identifies associations with 16 small non-coding sRNAs and 166 mRNAs. Meningococcal ProQ predominantly binds to highly structured regions and generally acts to stabilize its RNA targets. Loss of ProQ alters transcript levels of >250 genes, demonstrating that this minimal ProQ protein impacts gene expression globally. Phenotypic analyses indicate that ProQ promotes oxidative stress resistance and DNA damage repair. We conclude that FinO domain proteins recognize some abundant type of RNA shape and evolve RNA binding selectivity through acquisition of additional regions that constrain target recognition.

Introduction
Global post-transcriptional regulatory networks involving a central RNA-binding protein (RBP) and hundreds of mRNAs and small regulatory RNAs (sRNAs) have long been known in bacteria, centered on two RBP families, Csr/Rsm, and Hfq¹. The recent discovery of ProQ as another global RPB in Escherichia coli and Salmonella enterica² demonstrated that additional such networks exist, at least in γ-proteobacteria. ProQ was found to target a distinct set of sRNAs and mRNAs rivaling the target regulons of CsrA or Hfq in size^3,4. ProQ activity affects diverse pathways including motility and pathogenesis², and in Salmonella this RBP is required for full virulence⁵. [My emphasis]

Saskia Bauriedl, Milan Gerovac, Nadja Heidrich, Thorsten Bischler, Lars Barquist, Jörg Vogel, Christoph Schoen.
The minimal meningococcal ProQ protein has an intrinsic capacity for structure-based global RNA recognition.
Nature Communications, 2020; 11 (1) DOI: 10.1038/s41467-020-16650-6

Copyright: © 2020 The authors
Published open access by SpringerNature
Reprinted under a Creative Commons Attribution 4.0 International License (CC BY 4.0)

Obviously, this putative intelligent [sic] designer has put a lot of thought into this brilliant way to make humans, especially children and young adults, sick and die, or be left permanently disabled, and evidently very pleased with it's handiwork, it has used a similar method to make Escherichia coli and Salmonella enterica more virulent. This small protein enables the Meningococcal bacterium to repair its own DNA and to resist being killed by oxidation as well as activating some 250 genes, enabling the bacterium to bind itself to the cells of its victims more effectively.

Perhaps a creationist can explain how the putative designer of this piece of nastiness differs from a malevolent, anthropophobic psychopath. Tweet

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