Malevolent Designer News - How Ticks are Designed to Infect Deer With a Prion Disease

A wildlife camera captures deer practicing allogrooming — grooming one another to get places that they can’t reach on their own. During allogrooming, deer may eat ticks that contain CWD-infested blood.

Ticks may be able to spread chronic wasting disease between deer

White-tailed deer, Odocoileus virginianus
May catch fatal Chronic Wasting Disease from tics

Source: USDA Via Wikipedia
Public Domain

Black-legged or Deer tick,
Ixodes scapularis

Source: USDA via Wikipedia
Public Domain

The thing about being a troobuleeving creationist is that you have to find a way to avoid crediting your putative intelligent [sic] designer deity with all the nasties that exist in nature, while insisting that only your beloved intelligent [sic] designer designed everything.

You also need to buleeve your putative designer is omniscient because it's one and the same as the allegedly omniscient and omnipotent god of the Bible and Qur'an, so knows exactly what its designs will do when it designs them, which amounts to designing them for that purpose.

The same deity is also allegedly omni-benevolent, which makes parasites and prey-predator arms races difficult to explain, especially since it supposedly boasted to Isaiah about creating evil, so the Bible claims (Isaiah 45:7).

So, imagine the mental gymnastics that a troobuleeving creationist will need to perform to accommodate the knowledge that one of their intelligent [sic] designer's designs, the black-legged or deer tick, Ixodes scapularis, might be responsible for transmitting the prion that causes Chronic Wasting Disease (CWD) in deer, as this piece of research, led by Heather Inzalaco of the Wisconsin Cooperative Wildlife Research Unit, University of Wisconsin, Madison, USA, suggests.

The black-legged tick and how it transmits the rickettsia parasite, Anaplasma phagocytophilum to humans - The Malevolent Designer: Why Nature’s God is Not Good pp. 15-17.

First, a little about prions and the diseases they cause:

Prions are unique infectious agents composed of misfolded proteins that can cause a variety of neurodegenerative diseases in humans and animals. They are primarily associated with diseases known as transmissible spongiform encephalopathies (TSEs), which include conditions such as Creutzfeldt-Jakob disease (CJD) in humans, bovine spongiform encephalopathy (BSE or "mad cow disease") in cattle, and scrapie in sheep.

The term "prion" was first coined by Stanley B. Prusiner in 1982, who won the Nobel Prize in Physiology or Medicine in 1997 for his work on prion diseases. Prusiner proposed that prions are misfolded isoforms of a normal cellular protein called the prion protein (PrP). PrP is found in a healthy, properly folded conformation (PrP^C) in the cells of mammals, including humans. However, when it adopts an abnormal conformation (PrP^Sc), it becomes pathogenic and can trigger a chain reaction of misfolding in other PrP molecules.

The exact mechanism by which PrP^Sc induces disease is still not fully understood. However, it is believed that PrP^Sc has the ability to convert normal PrP^C into its misfolded form, leading to the accumulation of PrP^Sc aggregates. These aggregates can disrupt normal cellular functions, particularly in the central nervous system, resulting in neuronal damage, inflammation, and ultimately, the characteristic symptoms of prion diseases.

Unlike conventional infectious agents such as bacteria or viruses, prions lack genetic material (DNA or RNA). Instead, they propagate by templating the misfolding of normal PrP^C proteins into the abnormal PrP^Sc conformation. This ability to self-propagate and convert normal proteins into pathogenic forms is a unique characteristic of prions.

References:

1. Prusiner, S. B. (1998). Prions. Proceedings of the National Academy of Sciences, 95(23), 13363–13383. doi: 10.1073/pnas.95.23.13363
2. Aguzzi, A., & Calella, A. M. (2009). Prions: Protein aggregation and infectious diseases. Physiological Reviews, 89(4), 1105–1152. doi: 10.1152/physrev.00006.2009
3. Prusiner, S. B. (2012). Biology and genetics of prions causing neurodegeneration. Annual Review of Genetics, 46, 587–608. doi: 10.1146/annurev-genet-110711-155524

ChatGPT3 "What are prions and how do they cause diseases? With reference, please." [Response to user request] Retrieved from: https://chat.openai.com/

It's worth pointing out at this point that one of the cited reasons for believing there is an intelligent designer is that proteins need to be folded in precisely the right way to function correctly and, because there are so many different ways, in theory, a protein could be folded, the chance of it hitting the right one naturally is infinitesimally small, so there must have been intelligent agency. This is an example of the argument from ignorant incredulity and the false dichotomy fallacy, of course - which works on the ignorant and credulous targets of creationist frauds, but it leaves them to explain why their putative intelligent [sic] designer folded prions to do what they do.

The argument is nonsensical, of course, and even argues against intelligent design because what intelligent designer would come up with a design that means it needs to attend to the folding of every one of millions of proteins in every one of your trillions of cells, and every one of the countless trillions of cells in every one of billions of living species, and do it every time a cell divides, instead of designing a way to automate the process using the normal laws of chemistry and physics?
But that's yet another problem of their wackadoodle superstition for creationists to find a way to live with.

The findings of the research team led by Heather Inzalaco are explained in a University of Wisconsin - Maddison news release:

A new study from researchers at the University of Wisconsin–Madison finds that ticks can harbor transmissible amounts of the protein particle that causes chronic wasting disease (CWD), implicating the parasites as possible agents in the disease’s spread between deer in Wisconsin. The findings were published in the journal Nature.

CWD is caused by a pathogenic agent called a prion, which can pass from deer to deer through contact with things like prion-contaminated soil and infected bodily fluids such as urine, saliva, blood and feces. Prions, which cause disease in animals and in humans, prompt certain proteins to fold abnormally, particularly in the brain, and prevent these proteins from carrying out their normal functions. Over time, the CWD prion can cause severe brain damage and eventually death in deer.

A lot of CWD studies focus on the role soil plays in spreading the fatal neurological disease among deer. But Heather Inzalaco, a researcher in the Wisconsin Cooperative Wildlife Research Unit, housed in the UW–Madison Department of Forest and Wildlife Ecology, was curious about other potential environmental and behavioral means of transmission.

Deer live these secret lives; we don’t see everything that they do.

Deer will groom one another to get places that they can’t reach on their own through self-grooming. If they’re grooming each other and they’re doing that to remove ectoparasites [such as ticks], that might be problematic because they’re probably eating the ectoparasites.

Heather Inzalaco, lead author
Wisconsin Cooperative Wildlife Research Unit
Department of Forest and Wildlife Ecology
University of Wisconsin - Madison, Madison, WI, USA.

She started to consider what sort of things pester deer that could be connected to CWD: Ticks were the perfect parasitic potential culprit to investigate.

Ticks have a goal, of course, to feed on their host’s blood. Inzalaco began to wonder if ticks that acquire blood from CWD-infected deer could also host the prions and if so, could they contain enough prions to spread the disease.

The question became even more intriguing when she discovered that the most common non-aggressive social behavior that deer engage in is allogrooming.

First, she needed to show that ticks can take up and harbor these prions when they feed on CWD-infected blood. She designed an experiment to do just that.

You’d think that it’d be easy to get ticks to take a blood meal, but they are surprisingly fussy in the lab.

[Tics are] just like a little CWD Tic-Tac that are possibly being eaten by the deer,

Heather Inzalaco.

She was able to determine that ticks can not only carry the prions in their blood meal, they can also carry enough of the agent to potentially infect another animal with CWD. After seeing that the phenomenon was possible in the lab, it was time to see what was happening in the wild.

Inzalaco partnered with the Wisconsin Department of Natural Resources to study ticks collected from deer that hunters harvested and submitted for CWD testing. Of the 176 deer with ticks she studied, 15 of the deer were also positive for CWD. Inzalaco took the ticks from the infected deer and tested the blood they contained to quantify the amount of prion the ticks harbored.

She determined that these engorged, wild ticks did carry transmissible levels of prions — just like those in the lab — making them potential mechanical vectors for the disease.

We are all inextricably linked to ecosystem function and the biodiversity of those ecosystems. That is really what drives my desire to learn and do good science on a daily basis. We need to make an effort to preserve our natural heritage so that we can continue living on this planet and not be overtaken by disease and have healthy animals and healthy functioning ecosystems.

Heather Inzalaco.

The study did not test whether prion-carrying ticks did cause transmission to other deer. Understanding more about how CWD can spread can help improve the management of the disease. While it isn’t practical to treat all wild deer with tick preventatives, Inzalaco believes better land stewardship could help manage tick populations.

For instance, having contiguous habitat of native plant communities and properly managing areas to continue a natural fire regime has been shown to limit tick populations, she says, while more fragmented, unbalanced ecosystems riddled with invasive plants may allow ticks to proliferate more readily.

Inzalaco says it might be possible to use ticks as a way to screen for CWD in both wild and farmed deer. Current methods of diagnosis or screening involve invasive sample collection from animals or tissue sampling after their death. While testing the ticks from deer may not lead to the same level of accuracy as testing tissue samples, it could still be a useful tool to better understanding where the disease is affecting the deer population in the state.

Inzalaco also believes her research can help improve the ecosystems that everyone relies on, especially the state’s hunters.

The team's findings are published open access in the Nature journal Scientific Reports:

Chronic wasting disease (CWD) is a fatal neurodegenerative disease caused by infectious prions (PrP^CWD) affecting cervids. Circulating PrP^CWD in blood may pose a risk for indirect transmission by way of hematophagous ectoparasites acting as mechanical vectors. Cervids can carry high tick infestations and exhibit allogrooming, a common tick defense strategy between conspecifics. Ingestion of ticks during allogrooming may expose naïve animals to CWD, if ticks harbor PrP^CWD. This study investigates whether ticks can harbor transmission-relevant quantities of PrP^CWD by combining experimental tick feeding trials and evaluation of ticks from free-ranging white-tailed deer (Odocoileus virginianus). Using the real-time quaking-induced conversion (RT-QuIC) assay, we show that black-legged ticks (Ixodes scapularis) fed PrP^CWD-spiked blood using artificial membranes ingest and excrete PrP^CWD. Combining results of RT-QuIC and protein misfolding cyclic amplification, we detected seeding activity from 6 of 15 (40%) pooled tick samples collected from wild CWD-infected white-tailed deer. Seeding activities in ticks were analogous to 10–1000 ng of CWD-positive retropharyngeal lymph node collected from deer upon which they were feeding. Estimates revealed a median infectious dose range of 0.3–42.4 per tick, suggesting that ticks can take up transmission-relevant amounts of PrP^CWD and may pose a CWD risk to cervids.

Inzalaco, H.N., Bravo-Risi, F., Morales, R. et al.
Ticks harbor and excrete chronic wasting disease prions.
Sci Rep 13, 7838 (2023). https://doi.org/10.1038/s41598-023-34308-3

Copyright: © 2023 The authors.
Published by Springer Nature Ltd. Open access.
Reprinted under a Creative Commons Attribution 4.0 International license (CC BY 4.0)

So, what's it to be, Creationists: a malevolent designer busy designing ever more sophisticated way to make its creation suffer with parasites and prions and complex delivery systems like the black-legged tick, or am omnibenevolent god who either doesn’t know what some other supernatural designer is designing or is powerless to stop it?

It's time to grow up and deal with some of the many problems for your superstition, such as this one, even if that means you might have to consider the possibility of being wrong.

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Thank you for sharing!

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