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Original Article

The Assembly of Bacteriophage Functional Enzymatic Models in Association with E. coli Proteins’ Profiles

Journal of Biomedical Research & Environmental Sciences article abstract with citation details, DOI, publication dates, subject areas, full text links, and references.

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Open Access
Article Type Original Article
Subject Biology Group
OCLC 8940284028
Ayman A Elshayeb*, Amna Elfatih, Karimeldin MA Salih and Nada SE Mustafa
Issue: Volume1-Issue7
Pages: 320-329
Received: 2020-10-31
Accepted: 2020-11-18
Published: 2020-11-19

Abstract

Introduction: The invasion of bacteriophage on the associated host bacterium depends on their receptors’ orientation that adsorb them to cell surface. During phage replication a valuable number of proteins acts as lytic enzymes for host puncher at the beginning of the infection and other for burst after lytic cycle compilation. Accordingly, the proteomic relationship among phage and bacterium proteins could easily be studied by their protein profiles analysis.

Objective: To detect bacteriophages functional enzymes during lytic cycle.

Methods: The isolation and identification of Escherichia coli and their parasitic T7 phage group was done using bacterial culture and common plaque assay techniques. The investigations and protein-protein interactions’ assays were inveterate by proteins profile of phage and bacterium using Sodium Dodecyl Sulphate Poly Acrylamide Gel Electrophoresis (SDS-PAGE) to find out their molecular weights, where the scaled location of each mobile band was compared to the standards of identified proteins weights in the molecular ladder. Thereafter, Protein model’s assembly and bands migration was done by computer analytical software.

Results: Mobilization of the phage’ proteins inside the Two Dimensions (2D) gel ranged between 60 and 12 kDa where a model of 4 main bands with molecular weights of (46, 35, 24 and 14 kDa) is corresponded to the host ones, where pure 9 bands with molecular weight ranged between 96-24 kDa. The computational model analysis showed common shared molecular masses of 47, 34 and 16 kDa on plot area of the phage and the bacterium. Model interpretation confirmed that proteins ranged from 47.7 to 34.3 kDa resembles 43.3% of whole phage’s proteins that assembled the capsid head and the coil, while the molecular weight mass of 22.5 formed the tail’s proteins. The lytic enzymes’ molecular weight was ranged between 18-14 kDa according to the function of the enzyme. The study revealed that the 34 kDa band has the common shared peak between T7 phage group and associated Escherichia coli host.

Conclusion: Functional models of analysed proteins during phage assembly, ensures lytic enzymes are built in the capsid head and the lysozyme in the tail, they facilitate the enzymatic decay for bacterial host. This enzymatic function is related to the lytic cycle of the bacteriophages and their phenomenon in employing the bacterial DNA in proteins manufacturing during their replication inside host.

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© 2020 Elshayeb AA, et al. Distributed under Creative Commons CC-BY 4.0 Creative CommonsAttribution

How to cite this article

Elshayeb AA, Elfatih A, Salih KMA, Mustafa NSE. The Assembly of Bacteriophage Functional Enzymatic Models in Association with E. coli Proteins’ Profi les. J Biomed Res Environ Sci. 2020 Nov 19; 1(7): 320- 329. doi: 10.37871/jbres1162, Article ID: JBRES1162

Subject area(s)

MicrobiologyBiology

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