Stability of Bacteriophage T4 Short Tail Fiber

2000 ◽  
Vol 381 (3) ◽  
pp. 255-258 ◽  
Author(s):  
Martin R. Burda ◽  
Ingrid Hindennach ◽  
Stefan Miller
Keyword(s):  
Bacteriophage T4 ◽  
Tail Fiber ◽  
Tail Fiber Protein ◽  
Chemical Denaturation ◽  
E Coli ◽  
Short Tail ◽  
Fiber Protein ◽  
Equilibrium Unfolding ◽  
The Stability ◽  
Tail Fibers

Abstract Adsorption of Teven bacteriophages to the E. coli host cell is mediated by long and short tail fibers. Bacteriophage T4 short tail fiber protein p12 was used to investigate the stability against thermal and chemical denaturation. Purified p12 is thermostable with a melting point of 78C. Guanidinium chlorideinduced denaturation displayed strong hysteresis and an intermediate between 2 and 3 denaturant. The transitions occur at 1.5 and 3.2 denaturant as revealed by fluorescence spectroscopy and circular dichroism. The data suggest an equilibrium unfolding intermediate with a separate unfolding of the Cterminal knob domain and the shaft region.

scholarly journals Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34

Viruses ◽  
2017 ◽  
Vol 9 (7) ◽  
pp. 168 ◽  
Author(s):  
Meritxell Granell ◽  
Mikiyoshi Namura ◽  
Sara Alvira ◽  
Shuji Kanamaru ◽  
Mark van Raaij
Keyword(s):  
Crystal Structure ◽  
Bacteriophage T4 ◽  
Terminal Region ◽  
Tail Fiber ◽  
Tail Fiber Protein ◽  
Long Tail ◽  
Fiber Protein ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal

scholarly journals Unravelling the Links between Phage Adsorption and Successful Infection in Clostridium difficile

Viruses ◽  
2018 ◽  
Vol 10 (8) ◽  
pp. 411 ◽  
Author(s):  
Anisha Mahendra Thanki ◽  
Grace Taylor-Joyce ◽  
Ahmed Dowah ◽  
Janet Yakubu Nale ◽  
Danish Malik ◽  
...  
Keyword(s):  
Clostridium Difficile ◽  
Tail Fiber ◽  
Tail Fiber Protein ◽  
Irreversible Binding ◽  
Promising Alternative ◽  
Phage Adsorption ◽  
Phage Tail ◽  
Fiber Protein ◽  
Successful Infection ◽  
Tail Fibers

Bacteriophage (phage) therapy is a promising alternative to antibiotics for the treatment of bacterial pathogens, including Clostridium difficile. However, as for many species, in C. difficile the physical interactions between phages and bacterial cells have not been studied in detail. The initial interaction, known as phage adsorption, is initiated by the reversible attachment of phage tail fibers to bacterial cell surface receptors followed by an irreversible binding step. Therefore binding can dictate which strains are infected by the phage. In this study, we investigated the adsorption rates and irreversible binding of three C. difficile myoviruses: CDHM1, CDHM3 and CDHM6 to ten strains that represent ten prevalent C. difficile ribotypes, regardless of their ability to infect. CDHM1 and CDHM3 phage particles adsorbed by ~75% to some strains that they infected. The infection dynamics for CDHM6 are less clear and ~30% of the phage particles bound to all strains, irrespective of whether a successful infection was established. The data highlighted adsorption is phage-host specific. However, it was consistently observed that irreversible binding had to be above 80% for successful infection, which was also noted for another two C. difficile myoviruses. Furthermore, to understand if there is a relationship between infection, adsorption and phage tail fibers, the putative tail fiber protein sequences of CDHM1, CDHM3 and CDHM6 were compared. The putative tail fiber protein sequence of CDHM1 shares 45% homology at the amino acid level to CDHM3 and CDHM6, which are identical to each other. However, CDHM3 and CDHM6 display differences in adsorption, which highlights that there is no obvious relationship between putative tail fiber sequence and adsorption. The importance of adsorption and binding to successful infection is often overlooked, and this study provides useful insights into host-pathogen interactions within this phage-pathogen system.

Nonlytic Recombinant Phage Tail Fiber Protein for Specific Recognition of Pseudomonas aeruginosa

2018 ◽  
Vol 90 (24) ◽  
pp. 14462-14468 ◽  
Author(s):  
Yong He ◽  
Yanli Shi ◽  
Mengli Liu ◽  
Yingran Wang ◽  
Lin Wang ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Tail Fiber ◽  
Tail Fiber Protein ◽  
Recombinant Phage ◽  
Specific Recognition ◽  
Phage Tail ◽  
Fiber Protein

Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers 1 1Edited by P. E. Wright

2000 ◽  
Vol 301 (4) ◽  
pp. 975-985 ◽  
Author(s):  
Petr G Leiman ◽  
Victor A Kostyuchenko ◽  
Mikhail M Shneider ◽  
Lidia P Kurochkina ◽  
Vadim V Mesyanzhinov ◽  
...  
Keyword(s):  
Gene Product ◽  
Bacteriophage T4 ◽  
Short Tail ◽  
Tail Fibers

Tail Fiber Protein-Immobilized Magnetic Nanoparticle-Based Affinity Approaches for Detection of Acinetobacter baumannii

2019 ◽  
Vol 91 (15) ◽  
pp. 10335-10342 ◽  
Author(s):  
Yi-Ling Bai ◽  
Md. Shahed-Al-Mahmud ◽  
Karuppuchamy Selvaprakash ◽  
Nien-Tsung Lin ◽  
Yu-Chie Chen
Keyword(s):  
Acinetobacter Baumannii ◽  
Magnetic Nanoparticle ◽  
Tail Fiber ◽  
Tail Fiber Protein ◽  
Fiber Protein

The Short Tail-Fiber of Bacteriophage T4: Molecular Structure and a Mechanism for Its Conformational Transition

Virology ◽  
1993 ◽  
Vol 194 (1) ◽  
pp. 117-127 ◽  
Author(s):  
A.M. Makhov ◽  
B.L. Trus ◽  
J.F. Conway ◽  
M.N. Simon ◽  
T.G. Zurabishvili ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Conformational Transition ◽  
Bacteriophage T4 ◽  
Tail Fiber ◽  
Short Tail

scholarly journals Virulent Drexlervirial Bacteriophage MSK, Morphological and Genome Resemblance With Rtp Bacteriophage Inhibits the Multidrug-Resistant Bacteria

2021 ◽  
Vol 12 ◽  
Author(s):  
Muhammad Saleem Iqbal Khan ◽  
Xiangzheng Gao ◽  
Keying Liang ◽  
Shengsheng Mei ◽  
Jinbiao Zhan
Keyword(s):  
Multidrug Resistant ◽  
The Other ◽  
Structural Proteins ◽  
Resistant Bacteria ◽  
Tail Fiber ◽  
Lytic Bacteriophage ◽  
Tail Fiber Protein ◽  
Multidrug Resistant Bacteria ◽  
Genome Database ◽  
Fiber Protein

Phage-host interactions are likely to have the most critical aspect of phage biology. Phages are the most abundant and ubiquitous infectious acellular entities in the biosphere, where their presence remains elusive. Here, the novel Escherichia coli lytic bacteriophage, named MSK, was isolated from the lysed culture of E. coli C (phix174 host). The genome of phage MSK was sequenced, comprising 45,053 bp with 44.8% G + C composition. In total, 73 open reading frames (ORFs) were predicted, out of which 24 showed a close homology with known functional proteins, including one tRNA-arg; however, the other 49 proteins with no proven function in the genome database were called hypothetical. Electron Microscopy and genome characterization have revealed that MSK phage has a rosette-like tail tip. There were, in total, 46 ORFs which were homologous to the Rtp genome. Among these ORFs, the tail fiber protein with a locus tag of MSK_000019 was homologous to Rtp 43 protein, which determines the host specificity. The other protein, MSK_000046, encodes lipoprotein (cor gene); that protein resembles Rtp 45, responsible for preventing adsorption during cell lysis. Thirteen MSK structural proteins were identified by SDS-PAGE analysis. Out of these, 12 were vital structural proteins, and one was a hypothetical protein. Among these, the protein terminase large (MSK_000072) subunit, which may be involved in DNA packaging and proposed packaging strategy of MSK bacteriophage genome, takes place through headful packaging using the pac-sites. Biosafety assessment of highly stable phage MSK genome analysis has revealed that the phage did not possess virulence genes, which indicates proper phage therapy. MSK phage potentially could be used to inhibit the multidrug-resistant bacteria, including AMP, TCN, and Colistin. Further, a comparative genome and lifestyle study of MSK phage confirmed the highest similarity level (87.18% ANI). These findings suggest it to be a new lytic isolated phage species. Finally, Blast and phylogenetic analysis of the large terminase subunit and tail fiber protein put it in Rtp viruses’ genus of family Drexlerviridae.

Vergleichende Untersuchungen an teilchengebundenem und freiem T2- Lysozym und Kristallisierung beider Enzyme

1964 ◽  
Vol 19 (2) ◽  
pp. 129-133 ◽  
Author(s):  
W. Katz
Keyword(s):  
Enzymatic Activity ◽  
Gel Filtration ◽  
Crystalline Form ◽  
Small Extent ◽  
Tail Fiber ◽  
Tail Fiber Protein ◽  
Fiber Protein ◽  
Vergleichende Untersuchungen

Serological comparison between particle-bound T 2 phage lysozyme and lysozyme from T 2 phage lysates showed purified preparations of both enzymes to be contaminated to a small extent with T 2 tail fiber protein.The latter could be removed by gel filtration and does not possess enzymatic activity for its part.Both lysozymes have been obtained in crystalline form and were studied physico-chemically. They can be assumed to be identical.

scholarly journals Molecular Insights into Bacteriophage Evolution toward Its Host

Viruses ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 1132
Author(s):  
Marina de Leeuw ◽  
Maayan Baron ◽  
Oshrit Ben David ◽  
Ariel Kushmaro
Keyword(s):  
Host Recognition ◽  
Broad Host Range ◽  
Tail Fiber ◽  
Whole Genome ◽  
Tail Fiber Protein ◽  
Gene Encoding ◽  
Evolution And Development ◽  
Adaptation Mechanisms ◽  
Fiber Protein ◽  
Bacteriophage Evolution

Bacteriophages (phages), viruses that infect bacteria, are considered to be highly host-specific. To add to the knowledge about the evolution and development of bacteriophage speciation toward its host, we conducted a 21-day experiment with the broad host-range bacteriophage Aquamicrobium phage P14. We incubated the phage, which was previously isolated and enriched with the Alphaproteobacteria Aquamicrobium H14, with the Betaproteobacteria Alcaligenaceae H5. During the experiment, we observed an increase in the phage’s predation efficacy towards Alcaligenaceae H5. Furthermore, genome analysis and the comparison of the bacteriophage’s whole genome indicated that rather than being scattered evenly along the genome, mutations occur in specific regions. In total, 67% of the mutations with a frequency higher than 30% were located in genes that encode tail proteins, which are essential for host recognition and attachment. As control, we incubated the phage with the Alphaproteobacteria Aquamicrobium H8. In both experiments, most of the mutations appeared in the gene encoding the tail fiber protein. However, mutations in the gene encoding the tail tubular protein B were only observed when the phage was incubated with Alcaligenaceae H5. This highlights the phage’s tail as a key player in its adaptation to different hosts. We conclude that mutations in the phage’s genome were mainly located in tail-related regions. Further investigation is needed to fully characterize the adaptation mechanisms of the Aquamicrobium phage P14.

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