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7 results for “Bacteriophage Lambda”
Bacteriophage Lambda Structure at Atomic Resolution
<p>Bacteriophage Lambda structure at atomic resolution. This structure has been constructed in UCSF Chimera software putting together all the structures that compose bacteriophage lambda using cryoEM reconstructions and pdb structures. By Dr. Victor Padilla-Sanchez, PhD from Washington Metropolitan University. Email: drvictorpadilla@aol.com Website: https://www.drvictorpadillasanchez.com</p>
Data from: Ecological speciation of bacteriophage lambda in allopatry and sympatry
Understanding the conditions that allow speciation to occur is difficult because most research has focused on either long-lived organisms or asexual microorganisms. We propagated bacteriophage λ, a virus with rapid generations and frequent recombination, on two Escherichia coli host genotypes that expressed either the LamB or OmpF receptor. When supplied with either single host (allopatry), λ improved its binding to the available receptor while losing its ability to use the alternative. When evolving on both hosts together (sympatry), the viruses split into two lineages with divergent receptor preferences. Although the level of divergence varied among replicates, some lineages evolved reproductive isolation via genetic incompatibilities. This outcome indicates that, under suitable conditions, allopatric and sympatric speciation can occur with similar ease.
Data from: Ecological speciation of bacteriophage lambda in allopatry and sympatry
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Data from: Gain-of-function experiments in bacteriophage lambda uncover residues under diversifying selection in nature
Viral gain-of-function mutations frequently evolve during laboratory experiments. Whether the specific mutations that evolve in the lab also evolve in nature and whether they have the same impact on evolution in the real world is unknown. We studied a model virus, bacteriophage λ, that repeatedly evolves to exploit a new host receptor under typical laboratory conditions. Here we demonstrate that two residues of λ's J protein are required for the new function. In natural λ variants, these amino acid sites are highly diverse and evolve at high rates. Insertions and deletions at these locations are associated with phylogenetic patterns indicative of ecological diversification. Our results show that viral evolution in the laboratory mirrors that in nature and that laboratory experiments can be coupled with protein sequence analyses to identify the causes of viral evolution in the real world. Furthermore, our results provide evidence for widespread host-shift evolution in lambdoid viruses.
Data from: Gain-of-function experiments in bacteriophage lambda uncover residues under diversifying selection in nature
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Bacteriophage lambda overcomes a perturbation in its host‐viral genetic network through mutualism and evolution of life history traits
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High resolution view of bacteriophage lambda gene expression by ribosome profiling
GEO Series GSE47509. Escherichia coli str. K-12 substr. MG1655. 20 samples. Type: Expression profiling by high throughput sequencing.
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