P22 Phage Shows Promising Antibacterial Activity Under Pathophysiological Conditions&lt;strong&gt; &lt;/strong&gt;

Gildea, Logan; Ayariga, Joseph A.; Villafañe, Robert

doi:10.20944/preprints202111.0248.v1

Cited by 2 publications

(1 citation statement)

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“…Salmonella has been demonstrated to cause several acute and chronic infections in humans [1] . These bacteria is known to be responsible for over 1.2 million illnesses in the US each year [2, 3, 4, 5] .…”

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confidence: 99%

Proteolytic Analysis of Epsilon 34 Phage Tailspike protein indicates Partial Sensitivity to Proteinase K

Ayariga

Villafañe

2022

Preprint

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Purified bacteriophage Ɛ34 tailspike protein (Ɛ34 TSP) can bind to Salmonella newington (S. newington) via the binding site of the protein, which is the O antigens of the LPS of the bacterium. We demonstrated elsewhere that purified Ɛ34 TSP possessed bacteria lytic property on S. newington. The Ɛ34 TSP has been shown via computational prediction to consist of parallel β-helices like that of P22 TSP. These protein moieties are among the simplest repetitive structural elements in proteins. There exist extensive research on the folding behavior of β-helix proteins, which also provides insight on how amyloid fibrils are generated since these proteins consist of similar parallel β-helix motifs. One of the most significantly studied system for investigating protein folding is the from the Salmonella bacteriophage P22. The major component of this protein is a right-handed parallel β-helix with 13 rungs. Initial in silico analysis of the Ɛ34 phage TSP indicates similar structural similarity to the P22 TSP. Our previous studies indicated that despite the similarities of the two proteins, P22 TSP shows higher resistance to proteases (e.g. trypsin) and heat compared to Ɛ34 TSP. In this study we further proof that Ɛ34 TSP is partially sensitive to proteinase K, whereas P22 TSP is completely resistant to this protein. Detailed analysis indicates that specific structural motifs of Ɛ34 TSP is insensitive to the protease, whereas other regions of the protein showed susceptibility to it.

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Section: Introductionmentioning

confidence: 99%

Proteolytic Analysis of Epsilon 34 Phage Tailspike protein indicates Partial Sensitivity to Proteinase K

Ayariga

Villafañe

2022

Preprint

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Molecular Aspects of the Functioning of Pathogenic Bacteria Biofilm Based on Quorum Sensing (QS) Signal-Response System and Innovative Non-Antibiotic Strategies for Their Elimination

Juszczuk-Kubiak

2024

IJMS

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One of the key mechanisms enabling bacterial cells to create biofilms and regulate crucial life functions in a global and highly synchronized way is a bacterial communication system called quorum sensing (QS). QS is a bacterial cell-to-cell communication process that depends on the bacterial population density and is mediated by small signalling molecules called autoinducers (AIs). In bacteria, QS controls the biofilm formation through the global regulation of gene expression involved in the extracellular polymeric matrix (EPS) synthesis, virulence factor production, stress tolerance and metabolic adaptation. Forming biofilm is one of the crucial mechanisms of bacterial antimicrobial resistance (AMR). A common feature of human pathogens is the ability to form biofilm, which poses a serious medical issue due to their high susceptibility to traditional antibiotics. Because QS is associated with virulence and biofilm formation, there is a belief that inhibition of QS activity called quorum quenching (QQ) may provide alternative therapeutic methods for treating microbial infections. This review summarises recent progress in biofilm research, focusing on the mechanisms by which biofilms, especially those formed by pathogenic bacteria, become resistant to antibiotic treatment. Subsequently, a potential alternative approach to QS inhibition highlighting innovative non-antibiotic strategies to control AMR and biofilm formation of pathogenic bacteria has been discussed.

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P22 Phage Shows Promising Antibacterial Activity Under Pathophysiological Conditions<strong> </strong>

Cited by 2 publications

References 41 publications

Proteolytic Analysis of Epsilon 34 Phage Tailspike protein indicates Partial Sensitivity to Proteinase K

Proteolytic Analysis of Epsilon 34 Phage Tailspike protein indicates Partial Sensitivity to Proteinase K

Molecular Aspects of the Functioning of Pathogenic Bacteria Biofilm Based on Quorum Sensing (QS) Signal-Response System and Innovative Non-Antibiotic Strategies for Their Elimination

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