The Third Model of Richard Lenski's Experiment and the Ludicrous Evidence for Evolution
The third model of Richard Lenski’s experiment and the ludicrous evidence for evolution.
🪫 The Third Model of Richard Lenski’s Experiment and the Ludicrous Evidence for Evolution
Evolutionists argue that in this experiment, they used the bacteria-killing bacteriophage virus ,
and disabled the gene that produces the bacterial protein LamB , which the virus binds to infect the bacterial cell.
The virus then fixed mutations (modifications) in the J protein responsible for recognizing the bacterial cell,
leading to the recognition of another bacterial cell receptor, OmpF .
📌 “The processes responsible for the evolution of key innovations, whereby lineages acquire qualitatively new functions that expand their ecological opportunities, remain poorly understood.”
We examined how a virus — bacteriophage λ — evolved to infect its host, Escherichia coli , through a novel pathway.
Natural selection promoted the fixation of mutations in the virus’s host-recognition protein, J ,
that improved fitness on the original receptor, LamB ,
and set the stage for other mutations that allowed infection through a new receptor, OmpF .
These viral mutations arose only after the host evolved and reduced expression of LamB ,
whereas certain other host mutations prevented the phage from evolving the new function.
This study shows the complex interplay between genomic processes and ecological conditions
that favor the emergence of evolutionary innovations.
🪫 Translation :
“The processes responsible for the evolution of key innovations, by which lineages acquire qualitatively new functions that expand their ecological opportunities, remain poorly understood. We examined how a virus, the bacteriophage λ, evolved to infect its host, Escherichia coli, through a novel pathway. Natural selection promoted the fixation of mutations in the virus’s host recognition protein, J, that improved fitness over the original receptor, LamB, and paved the way for other mutations that allowed infection through a new receptor, OmpF. These viral mutations arose only after the host had evolved and reduced the expression of LamB, while some other host mutations prevented the bacteriophage from evolving the new function. This study demonstrates the complex interplay between genomic processes and environmental conditions that drive the emergence of evolutionary innovations.”
🪫 So far you might think this is evolution; but hold on…
🧠 ★ First:
The bacteria reduced the expression of the gene responsible for producing the protein LamB
to which the virus binds.
- These viral mutations arose only after the host evolved, reducing the expression of LamB .
🪫 This means it is not evolution.
What happened next?
The virus modified the protein that recognizes the bacterial receptor LamB
by substituting an adenine for a guanine (A to G ) at position 3034,
so that it recognizes another structurally similar receptor, OmpF .
🧬 In short:
The protein (J ) that recognizes the bacterial receptor LamB was modified,
and it now recognizes the bacterial receptor OmpF ,
meaning it can match both sites, or only one after the modification,
which is structurally similar to the first.
This is similar to the multifunctional enzyme system (Promiscuous Enzyme) ,
which can interact with more than one ligand similar to the active site.
We previously demonstrated this in the example of nylon-digesting Flavobacteria .
🔬 We sequenced the genome of the evolved phage EvoC in order to identify the mutations
that allowed it to use the OmpF receptor (16).
There were five mutations in total, and all of them were in the J gene (Fig. 2).
Targeted sequencing of J showed that a single substitution (A to G at position 3034)
differentiated EvoC from another evolved isolate from the same time point, EvoA ,
that could use only the ancestral LamB receptor,
indicating that mutation contributed to the new receptor function.
Another LamB-dependent phage from the same day, EvoB , differed from EvoC at five sites in the J protein .
🪫 Although OmpF has the most similar crystal structure to LamB of any E. coli protein determined to date (29),
they are not the most similar pair in terms of amino acid sequence (table S3).
This discordance suggests that overall structure is at least as important for λ binding
as the identity of specific amino acid residues.
🪫 Even more ironic:
They interpreted this as parallel evolution . 🤡
There are four striking cases of parallel evolution of the J protein in the phage that target OmpF. Study:
https://pmc.ncbi.nlm.nih.gov/articles/PMC3306806/
Quick fact: According to evolution, humans did not evolve from chimpanzees, but rather from a chimpanzee-like ape. As for humans and chimpanzees, they have the same ancestor (they evolved from a common ancestor), according to evolution.
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https://pmc.ncbi.nlm.nih.gov/articles/PMC3306806/
Repeatability and Contingency in the Evolution of a Key Innovation …
The processes responsible for the evolution of key innovations, whereby lineages acquire qualitatively new functions that expand their ecological opportunities, remain poorly understood. We examined how a virus, bacteriophage λ, evolved to infect …
