Latrodectus hesperus female with egg sac.
Black widow spiders have a cocktail of toxins, most of which are effective against their arthropod prey such as insects, but one of them, α-latrotoxin, is very effective against vertebrates, including humans, although even the smallest vertebrates don't normally feature in the black widow's diet.
So why did this toxin evolve?
Normally, a species which is capable of delivering a nasty, even lethal, bite to a threat, rather than to prey, evolves strategies for avoiding doing so, while warning that it could if it wanted to - rather like a creationists avoiding answering a question while pretending they could if they wanted to, only without the pretense. Most species do this with warning colours or, in the case of the rattlesnake, a warning rattle. This is because using venom against a threat might mean there isn't enough left if the next potential meal wanders by, so it's better to warn and threaten than to actually bite.
But not so the black widow, except for the strikingly marked European species, Latrodectus tredecimguttatus, and the South American, Latrodectus curacaviensis. If anything, the black widow is cryptocamoflaged to not be noticed in the dark places they inhabit.
What can you tell me about black widow spiders, how their toxins evolved and why one, α-latrotoxin, targets the mammalian nervous system? Black widow spiders (Latrodectus spp.) are among the most well-known venomous spiders. Their venom contains a mix of neurotoxic proteins, including the potent toxin α-latrotoxin, which specifically affects the nervous system. The evolution of their venom, including α-latrotoxin, likely involves adaptations for prey capture and defense. Over time, spiders like the black widow have fine-tuned their venom to subdue a variety of prey, including insects and sometimes vertebrates.It could be that a predator quickly leans to avoid them after once being bitten by a black widow, but that means the spider has to use some precious toxin while there is a substantial risk of actually being killed in the exchange.
Evolution of Black Widow Venom
Black widow venom is a complex cocktail of proteins and peptides, many of which target the nervous systems of their prey. As predators of insects, *Latrodectus* spiders evolved toxins to immobilize and kill small arthropods. However, black widows also encounter vertebrates as both predators and threats, which likely contributed to the evolution of some toxins that work across different phyla.
The venom's key neurotoxins act on neurotransmitter release mechanisms. In particular, black widows produce toxins targeting calcium channels, which control neurotransmitter release in both invertebrate and vertebrate nervous systems. This widespread functionality reflects a co-evolutionary arms race between predators and prey, where venom needs to be effective against different nervous system architectures.
Why α-Latrotoxin Targets the Mammalian Nervous System
α-Latrotoxin is one of the most studied components of black widow venom and is particularly interesting because of its high specificity for vertebrate synapses, including mammals. This toxin triggers massive exocytosis (release) of neurotransmitters, causing muscle spasms, pain, and paralysis.
- Mechanism of Action: α-Latrotoxin binds to receptors on the surface of nerve cells, like neurexins and latrophilins, found specifically in vertebrates. Upon binding, it triggers the influx of calcium ions, which leads to the uncontrolled release of neurotransmitters such as acetylcholine, glutamate, and dopamine.
- Evolutionary Hypothesis: The evolutionary reason why α-latrotoxin targets the mammalian nervous system might be linked to both defensive and accidental interactions. Black widow spiders may not have evolved the toxin specifically for mammalian prey but rather to deter vertebrate predators like birds or small mammals that could threaten the spider. Given that toxins evolve under pressure for survival and defense, a broader target range—including vertebrates—would provide more protection.
The interaction of α-latrotoxin with the mammalian nervous system is probably an evolutionary side effect. As the toxin evolved for general efficacy in subduing prey and deterring predators, it incidentally found vertebrate nervous systems susceptible, possibly due to conserved mechanisms in neurotransmitter release across taxa.
Why Black Widows Produce Neurotoxins
The primary evolutionary advantage of neurotoxins, like α-latrotoxin, is their ability to quickly incapacitate prey, ensuring that the spider can safely feed. Additionally, these toxins serve as a strong defense against potential predators. In black widow spiders, their venom is potent even in minute amounts, suggesting an evolutionary emphasis on efficiency—injecting a small amount of venom for a large effect.
In summary, α-latrotoxin probably evolved as part of a broad-spectrum venom that could paralyze a wide range of potential threats and prey. Its specificity for the mammalian nervous system reflects evolutionary "side effects" of targeting widely conserved molecular pathways involved in neurotransmitter release.
Using toxin as a deterrent tends to be avoided with most venomous species which use warning to avoid it. Why would the black widow be different in that respect?
You're right that most venomous species rely on warning signals, such as bright colors, to deter potential predators rather than using their venom offensively as a deterrent. This strategy is generally energy-efficient since producing venom is metabolically expensive, and using it purely for defense can deplete reserves that could be used for capturing prey. However, black widow spiders (*Latrodectus* spp.) seem to represent an exception to this general trend. Here are some possible reasons why black widows might rely more on venom for defense and differ from species that use warning signals:In summary, black widow spiders may rely on venom for defense instead of warning coloration due to their cryptic nature, nocturnal habits, static web habitat, small size, and potentially unavoidable encounters with predators. Their highly potent venom is likely an evolved "last resort" defense that compensates for these factors, making them an outlier among venomous species that use warnings or avoidance strategies to deter predators.
- Cryptic Behavior and Camouflage
Black widow spiders are typically not brightly colored like many species that use aposematism (warning coloration). Instead, they tend to be cryptic, often hiding in dark, undisturbed areas. The females are usually black with a small red hourglass marking on their abdomen, which isn't immediately visible unless you’re close to the spider. This lack of conspicuous warning signals makes it harder for potential predators to recognize them as dangerous. Since they don’t use warning colors, they might rely more on defensive venom if they are discovered.- Nocturnal and Solitary Lifestyle
Black widows are largely nocturnal and prefer to stay hidden during the day. This reduces their likelihood of being seen by predators but increases the chances of surprise encounters at night when visual warning signals are less effective. In a dark or low-visibility environment, relying on defensive venom may be more advantageous than visual warnings, since a predator might stumble upon the spider without ever noticing the small hourglass marking.
Additionally, black widows are solitary creatures, unlike some venomous species that may live in social groups or have other forms of protection. Since each spider is on its own, it cannot afford to rely on communal defense mechanisms or social learning (as other animals do), which would promote the effectiveness of warning signals. This solitary nature may favor an aggressive venom-based defense.- Burrowed and Static Web Habitat
Black widows construct their webs in sheltered, low-traffic areas like under rocks, wood piles, or crevices, and they are relatively sedentary. This static web-based lifestyle means the spider might not have the luxury of running away from threats as easily as more mobile species. Since they can’t escape easily, they might rely more on their venom as a last line of defense if a predator or threat happens upon their web.- Small Size and Vulnerability
Black widows are relatively small and vulnerable compared to larger spiders. They don’t have the size or strength to physically fight off predators, so venom becomes their primary method of self-defense. In contrast, larger animals or venomous snakes might have the ability to intimidate or warn off predators through size or posturing. The smaller black widow might have no choice but to use venom when threatened, as physical intimidation or escape is not as feasible.- High Potency, Low Volume Venom
The venom of black widows is extraordinarily potent, but they don’t produce it in large quantities. This might suggest that black widows evolved to rely on extremely efficient, small doses of venom that can paralyze or kill quickly. Since their venom works rapidly on the nervous systems of both prey and predators, it would serve as a highly effective "last-resort" defense when a warning strategy fails or isn’t available.- Predators May Not Be Deterrable
Some predators of black widow spiders, like certain birds or reptiles, may not be easily deterred by visual warning signals, particularly if they have poor color vision or are opportunistic feeders. Additionally, some animals may not have learned to associate black widow markings with danger, especially if encounters are rare in the local population. In such cases, relying on venomous defense is more critical.- Limited Reproductive Opportunities
Female black widows invest heavily in reproduction, and many are highly sedentary once they establish a web. Losing a web or succumbing to predation can represent a significant loss of reproductive potential for these spiders. Therefore, they may be more willing to use venom as a defense in order to protect their reproductive future, even though it is costly, rather than abandoning their web or risking injury.
Typically, how quickly does the α-latrotoxin act against vertebrates?
α-Latrotoxin, the primary neurotoxic component of black widow venom, acts relatively quickly once injected into vertebrates, including humans. However, the onset of symptoms depends on several factors, such as the dose of venom, the size of the animal or human affected, and the location of the bite. Typical Onset of Symptoms
In humans and other vertebrates, the effects of α-latrotoxin generally begin to manifest within 10 to 60 minutes after envenomation. This rapid onset is due to the toxin's ability to cause massive neurotransmitter release from nerve terminals, leading to various neurological and muscular symptoms. The following process occurs:
- Binding and Activation (within minutes): α-Latrotoxin binds to specific receptors on presynaptic nerve terminals, such as neurexins and latrophilins. This binding starts a cascade that increases calcium influx, which in turn leads to the release of neurotransmitters like acetylcholine, glutamate, and norepinephrine.
- Neurotransmitter Release (within minutes to an hour): The massive, unregulated release of neurotransmitters into the synaptic cleft results in overstimulation of muscles, leading to muscle spasms, cramps, and pain.
Symptom Progression in Humans
- Immediate Symptoms (10–30 minutes): Initial pain, swelling, and localized muscle cramps occur near the site of the bite. The pain may radiate to larger muscle groups, such as the abdomen, chest, or legs, depending on the bite location.
- Systemic Symptoms (30 minutes to a few hours): As the toxin spreads, more severe symptoms can develop. These include intense muscle spasms, rigidity, sweating, nausea, hypertension, and in severe cases, difficulty breathing. This phase is often called latrodectism, and it reflects the systemic effects of the toxin on the nervous system.
Peak Effects (3–6 hours)
Most of the intense symptoms tend to peak within 3 to 6 hours after the bite. However, for some individuals, especially those who are more sensitive to the venom (such as children or the elderly), symptoms may persist for up to 24–48 hours without medical intervention.
Mechanism and Recovery
While the symptoms can be quite severe, α-latrotoxin does not cause permanent damage to the nervous system in most cases. The body eventually recovers as the overactive nerve terminals "reset" and neurotransmitter levels stabilize, often with the help of medical treatments such as antivenom, muscle relaxants, and pain relief medications. Full recovery usually occurs within a few days to a week.
In summary, α-latrotoxin acts quickly, with symptoms typically beginning within 10–60 minutes and peaking within a few hours. Its fast action is due to its ability to rapidly trigger the release of neurotransmitters, leading to painful and systemic neurological symptoms in vertebrates.
Time enough to kill and eat the spider?
Yes, in theory, there is time for a predator to kill and eat a black widow spider before the α-latrotoxin takes full effect. The onset of severe symptoms in vertebrates, such as mammals or birds, typically occurs within 10 to 60 minutes, with the most intense effects peaking hours later. This means that a predator could potentially consume the spider long before the full effects of the venom incapacitate it.
However, many predators may still avoid eating black widows despite this delay in venom effects for a few reasons:
- Pain at the Bite Site
Even though the systemic effects of the venom take time to develop, the bite site often becomes painful almost immediately, which might cause the predator to release or avoid the spider after being bitten. If the predator feels discomfort right away, it may abandon the prey before finishing the meal.- Learned Avoidance
Some animals learn to avoid black widows due to previous negative experiences. While the venom may not incapacitate them quickly enough to stop them from eating a spider once, the pain or discomfort that follows the encounter may discourage future attempts. Predators that have encountered black widows and experienced these symptoms might recognize them based on their appearance or behavior and avoid them altogether.- Risk-Reward Tradeoff
Many animals that eat spiders may not rely on any one individual for sustenance, so the risk of encountering a venomous species like a black widow may not be worth it. If the predator recognizes the spider as potentially dangerous, it may choose easier prey, even if it could theoretically kill and consume the black widow before feeling the effects of the venom.- Protective Web Positioning
Black widows tend to construct their webs in low-traffic, sheltered areas, which may reduce the likelihood of encounters with large predators. Their choice of hidden locations could decrease the chances that a predator will notice and eat them in the first place, reducing the need for an immediate venomous defense.
Conclusion
While a predator could certainly kill and eat a black widow spider before the α-latrotoxin venom fully affects its nervous system, the spider's defenses are multifaceted. Immediate pain from the bite, learned avoidance, and the spider's cryptic lifestyle all help reduce the likelihood of a successful predation attempt.
For a discussion on this see the AI panel to the right:
My best guess is that there were two possible ways this evolved:
- Altruism: The benefits of delivering a painful bite even though the spider gets eaten is that the predators gets a dose of aversion therapy that deters if from eating the spider's descendants and close relatives in the local environment, so the genes for this altruistic behaviour tend to predominate in the gene pool. This is similar to the explanation for the male being eaten by the female in that a free meal for her gives the eggs carrying his genes a better chance of surviving.
- Serendipity: The toxin evolved to be effective against a prey species and just happened to be effective against the vertebrate nervous system, after all the basic physiology of how nerve cells and synaptic neurotransmitters work is similar in arthropods and vertebrates. Now there is no selection pressure to remove it.
Certainly, the mechanism of toxicity of α-latrotoxin, discovered by a team of researchers at the University of Münster, Germany, is what creationists would describe as irreducibly complex, and it's difficult to see how it could possibly be described as the result of 'genetic entropy' and 'devolution' [sic] - the favourite excuse for harmful things that look designed but for which creationists wish to absolved their putative creator of responsibility.
The Münster team have just published their findings, open access, in the journal Nature Communications and announced it in a University of Münster press release:
Scientists decode black widow spider venom
Cryo-EM and MD simulations unveil the mechanism of the potent neurotoxin α-latrotoxin in forming calcium-permeable membrane pores.
The black widow spider is one of the most feared spider species. Its venom is a cocktail of seven different toxins that attack the nervous system. These so-called latrotoxins specifically paralyse insects and crustaceans, but one of them, the α-latrotoxin, targets vertebrates and is also poisonous to humans. It interferes with the transmission of signals in the nervous system. As soon as α-latrotoxin binds to specific receptors of the synapses – the contacts between nerve cells or between nerve cells and muscles – calcium ions flow uncontrollably into the presynaptic membranes of the signalling cells. This induces release of neurotransmitters, triggering strong muscle contractions and spasms. Despite the apparent simplicity of this process, there is a highly complex mechanism behind it. Scientists at the University of Münster have now deciphered the structure of α-latrotoxin before and after membrane insertion at near atomic resolution.
In order to better understand the mechanism of calcium influx into the presynaptic membrane, experts from the Center for Soft Nanoscience at the University of Münster, headed by Prof Christos Gatsogiannis (Institute of Medical Physics and Biophysics) and Prof Andreas Heuer (Institute of Physical Chemistry), used high-performance cryo-electron microscopy (cryo-EM) and molecular dynamics (MD) computer simulations. They showed that the toxin undergoes a remarkable transformation when it binds to the receptor. Part of the toxic molecule forms a stalk that penetrates the cell membrane like a syringe. As a special feature, this stalk forms a small pore in the membrane that functions as a calcium channel. MD simulations revealed that calcium ions can flow into the cell through a selective gate located on the side directly above the pore.
When the α-latrotoxin binds to the receptor of the presynaptic membrane of the signalling cell, it undergoes a transformation: part of the molecule forms a stalk that penetrates the cell membrane (“membrane insertion”, fig. right). As a special feature, this stalk forms a small pore in the membrane that acts as a calcium channel. MD simulations revealed that calcium ions (Ca2+ ions) enter the cell through a lateral selective gate directly above the pore.© Uni MS - Gatsogiannis group
Thanks to these results, researchers now better understand how α-latrotoxin works.
The toxin mimics the function of the calcium channels of the presynaptic membrane in a highly complex way. It therefore differs in every respect from all previously known toxins.
Professor Christos Gatsogiannis, co-corresponding author
Institute for Medical Physics and Biophysics
University Münster, Münster, Germany.
The new findings open up a wide range of potential applications; latrotoxins have considerable biotechnological potential, including the development of improved antidotes, treatments for paralysis and new biopesticides.
The research results have just been published in the journal Nature Communications. In previous work, the research group led by Christos Gatsogiannis had already deciphered the structure of insect-specific latrotoxins in the venom of the black widow spider before inserting into the membrane.
publication:BU Klink, A Alavizargar, KK Subramaniam, M Chen, A Heuer, C Gatsogiannis (2024)
Structural basis of α-latrotoxin transition to a cation selective pore. Nature Communications 15, 8551; DOI: 10.1038/s41467-024-52635-5
AbstractAlthough the evolutionary reason for black widow spiders having a toxin which is potentially lethal to vertebrates when they are not a prey species for the spider, may be obscure with a few plausible theories to explain it, it is an even bigger problem for creationists.
The potent neurotoxic venom of the black widow spider contains a cocktail of seven phylum-specific latrotoxins (LTXs), but only one, α-LTX, targets vertebrates. This 130 kDa toxin binds to receptors at presynaptic nerve terminals and triggers a massive release of neurotransmitters. It is widely accepted that LTXs tetramerize and insert into the presynaptic membrane, thereby forming Ca2+-conductive pores, but the underlying mechanism remains poorly understood. LTXs are homologous and consist of an N-terminal region with three distinct domains, along with a C-terminal domain containing up to 22 consecutive ankyrin repeats. Here we report cryoEM structures of the vertebrate-specific α-LTX tetramer in its prepore and pore state. Our structures, in combination with AlphaFold2-based structural modeling and molecular dynamics simulations, reveal dramatic conformational changes in the N-terminal region of the complex. Four distinct helical bundles rearrange and together form a highly stable, 15 nm long, cation-impermeable coiled-coil stalk. This stalk, in turn, positions an N-terminal pair of helices within the membrane, thereby enabling the assembly of a cation-permeable channel. Taken together, these data give insight into a unique mechanism for membrane insertion and channel formation, characteristic of the LTX family, and provide the necessary framework for advancing novel therapeutics and biotechnological applications.
Introduction
Latrotoxins (LTXs) are the main toxic components of the venom of black widow spiders (Latrodectus)1. The venom includes the vertebrate-specific α-latrotoxin (α-LTX)2,3, five insecticidal toxins known as α, β, γ, δ, and ε-latroinsectotoxins (LITs)4,5,6, as well as a toxin specific to crustaceans named α-latrocrustatoxin (α-LCT)7. Upon envenomation, LTXs impact the victim’s nervous system by triggering massive neurotransmitter release upon binding to receptors8,9,10,11,12. α-LTX has been widely used as a molecular tool to study the exocytosis of synaptic vesicles and its actions are considered precisely the opposite of those of botulinum and tetanus toxins, both of which inhibit instead of activating the same secretory apparatus13.
LTXs are large proteins, ranging from 110 kDa to 140 kDa, and they share a common architecture consisting of an N-terminal region containing functionally important cysteines and a C-terminal domain with up to 22 ankyrin repeats (ARs)14,15. The mature toxins are created from non-toxic precursors by posttranslational cleavage of a short N-terminal and a larger C-terminal domain by Furin-like proteases16. In solution, LTXs exist as monomers or dimers17,18,19. However, in the presence of calcium (Ca2+) or magnesium ions (Mg2+), they have been observed to spontaneously oligomerize and integrate into the membrane, forming tetrameric pores that allow the selective passage of cations18. The efficiency of this process is significantly increased in the presence of receptors20. Recently, we reported electron cryo-microscopy (cryo-EM) structures of both the α-LCT monomer and the δ-LIT dimer, shedding light on the overall domain organization of the LTX family19. However, the mechanism of LTX pore formation remained elusive, as we currently lack detailed structures of LTX tetramers, and pore events have only been visualized at low resolution18. Understanding the mechanism of LTX action holds significant medical relevance21,22 and the potential to lead to the development of biotechnological applications and biopesticides23.
Here, we show cryo-EM structures of the α-LTX tetramer in both the prepore and pore states. Combined with AlphaFold2 structural predictions and MD simulations, we elucidate the long-sought-after α-LTX pore and unveil a unique mechanism characterized by dramatic conformational changes during α-LTX transition into a cation-selective channel.
Fig. 1: Cryo-EM structure of α-LTX in two distinct tetrameric states.
a 2D class averages from datasets measured at different stage tilts. At low tilt angles, the presence of two distinct tetrameric states becomes apparent. Note the difference in diameter of the central channel. b Maps of the prepore (gray) and pore (yellow) state. For one monomer each, the derived molecular model is shown. c Molecular models of prepore and pore state of α-LTX. The side views depict two opposing subunits, colored according to their domain organization, as shown in the respective scheme. The first ~100 residues of the CD (“tip of the needle”) are not resolved in the pore structure. CD connector domain, HBD helical bundle domain, ARD ankyrin-like repeat domain, PD plug domain.
Fig. 2: Molecular architecture of the α-LTX pore.
a Representative α-LTX particle on a POPC-liposome in negative stain EM. From 988 micrographs, a total of 108 similar particles were used to create a 2D class average as shown in (b). The individual domains of the toxins are highlighted (CD connector domain, HBD helical bundle domain, PD β-sheet plug domain, ARD ankyrin repeat domain). c AlphaFold2 prediction of a tetrameric assembly of residues E21–E360 of α-LTX. The surface coulombic electrostatics [kcal/(mol·e)] indicates a membrane-spanning domain at its N-terminus. d Molecular model of the complete α-LTX pore obtained by combining the cryo-EM structure and the AlphaFold2 prediction overlaid in the negative stain average of α-LTX pore on liposomes. e Structural rearrangements of the CD lead to the formation of an extended coiled-coil and the TMD.
Fig. 3: MD simulations of the pore structure of α-LTX.
a Cartoon representation of the pore structure of α-LTX (residues E21–E360). The pore is represented as an orange surface. Residues facing the pore volume are represented as sticks with labels colored according to their biochemical properties. The pore profiles from the two simulations (residues C91–Y260 for the upper part and the stalk; residues E21–S116 for the membrane protein part) are shown as blue and orange lines, respectively. b Cartoon representation of the Na+ and Ca2+ positions in the HBD, respectively, obtained from a superposition of many simulation snapshots with an applied electric field. Also, the resulting pore radius is shown together with its standard deviation. c Representative ion trajectories, correspond to typical permeation events of the TMD by Na+ and Ca2+ ions, with and without an applied electric field. Additionally, shown are ion density profiles obtained by averaging all successful permeation events. d Cartoon representations of simulations of the membrane part with different ions (Na+, Ca2+, La3+, and Cl−) with a superposition analogous to b. The Ca2+ ionic densities in different slabs in the xy-plane are shown (5 Å and 10 Å widths along z, respectively).
Fig. 4: α-LTX stabilization by cysteines and disulfide bonds.
a Position of cysteines in α-LTX. Disulfide pairs (CC1–CC4) are marked with braces. b CD in the prepore state. The interacting AR domain is contoured by its surface hydrophobicity. c CD in the pore state. The interacting CDs from different α-LTX monomers are contoured by surface hydrophobicity. d, e Cys413 and disulfide bonds in the AR domain. The prepore state is colored and the pore state in light gray.Fig. 5: Schematic model of α-LTX activation, tetrameric prepore assembly, and transition to a cation permeable channel.
The precursor of α-LTX is activated by proteolytic cleavage of its inhibitory terminal domains in the venom gland. Tetramerization, a prerequisite for pore formation, may be enhanced through association with presynaptic receptors. A central Ca2+ binding site brings the HBD domains into close proximity. The C-terminal helices of the HBDs, along with the CD domains, reorient to form a tetrameric coiled-coil stalk. The N-terminal helices of this stalk, stabilized by disulfide bridges, insert into the membrane, forming a cation-permeable transmembrane channel.Klink, B.U., Alavizargar, A., Kalyankumar, K.S. et al. Structural basis of α-latrotoxin transition to a cation-selective pore. Nat Commun 15, 8551 (2024). https://doi.org/10.1038/s41467-024-52635-5
Copyright: © 2024 The authors.
Published by Springer Nature Ltd. Open access.
Reprinted under a Creative Commons Attribution 4.0 International license (CC BY 4.0)
It can't be easily dismissed with the idiotic notion of 'genetic entropy' and the even more idiotic notion of 'devolution', and, if evolution by natural selection is ruled out, as it has to be by creationists dogma, that only leaves creationists with their favourite explanation - intelligent [sic] design.
In other words, if this toxin is not the result of a mindless process in which no gods were involved, according to creationists it must be due to the malevolent intent of a designer, since there appears to be no discernible benefit to the victims of the spider's bite, and an omniscient designer would have been fully aware of what it would do to vertebrates when it designed it.
So, a simple binary choice for creationists: evolution or design with malevolent intent?
The Malevolent Designer: Why Nature's God is Not Good
This book presents the reader with multiple examples of why, even if we accept Creationism's putative intelligent designer, any such entity can only be regarded as malevolent, designing ever-more ingenious ways to make life difficult for living things, including humans, for no other reason than the sheer pleasure of doing so. This putative creator has also given other creatures much better things like immune systems, eyesight and ability to regenerate limbs that it could have given to all its creation, including humans, but chose not to. This book will leave creationists with the dilemma of explaining why evolution by natural selection is the only plausible explanation for so many nasty little parasites that doesn't leave their creator looking like an ingenious, sadistic, misanthropic, malevolence finding ever more ways to increase pain and suffering in the world, and not the omnibenevolent, maximally good god that Creationists of all Abrahamic religions believe created everything. As with a previous book by this author, "The Unintelligent Designer: Refuting the Intelligent Design Hoax", this book comprehensively refutes any notion of intelligent design by anything resembling a loving, intelligent and maximally good god. Such evil could not exist in a universe created by such a god. Evil exists, therefore a maximally good, all-knowing, all-loving god does not.
Illustrated by Catherine Webber-Hounslow.
Available in Hardcover, Paperback or ebook for Kindle
Illustrated by Catherine Webber-Hounslow.
The Unintelligent Designer: Refuting The Intelligent Design Hoax
ID is not a problem for science; rather science is a problem for ID. This book shows why. It exposes the fallacy of Intelligent Design by showing that, when examined in detail, biological systems are anything but intelligently designed. They show no signs of a plan and are quite ludicrously complex for whatever can be described as a purpose. The Intelligent Design movement relies on almost total ignorance of biological science and seemingly limitless credulity in its target marks. Its only real appeal appears to be to those who find science too difficult or too much trouble to learn yet want their opinions to be regarded as at least as important as those of scientists and experts in their fields.
Available in Hardcover, Paperback or ebook for Kindle
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