Morphologically Different Pectobacterium brasiliense Bacteriophages PP99 and PP101: Deacetylation of O-Polysaccharide by the Tail Spike Protein of Phage PP99 Accompanies the Infection

Monoclonal antibodies that detect folding intermediates in vitro were used to monitor the appearance of folded polypeptide chains during their synthesis on the ribosomes. Nascent immunoreactive chains of the bacteriophage P22 tail-spike protein and of the Escherichia coli β 2 subunit of tryptophan-synthase were thus identified, suggesting that they can fold on the ribosomes. Moreover, the immunoreactivity of ribosome- bound tryptophan-synthase β-chains of intermediate lengths was shown to appear with no detectable delay compared to their synthesis. This suggested that β-chains start folding during their elongation on the ribosomes. However, newly synthesized incomplete β-chains were shown to interact with chaperones while still bound to the ribosome. Because of the peculiar properties of the epitope recognized by the anti- tryptophan-synthase monoclonal antibody used, it could not be concluded whether the immunoreactivity of the nascent β-chains resulted from their ability to fold cotranslationally or from their association with chaperones which might maintain them in an unfolded, immunoreactive state.

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Role of bacteriophage SPP1 tail spike protein gp21 on host cell receptor binding and trigger of phage DNA ejection

Molecular Microbiology ◽

10.1111/j.1365-2958.2011.07931.x ◽

2011 ◽

Vol 83 (2) ◽

pp. 289-303 ◽

Cited By ~ 39

Author(s):

Inês Vinga ◽

Catarina Baptista ◽

Isabelle Auzat ◽

Isabelle Petipas ◽

Rudi Lurz ◽

...

Keyword(s):

Host Cell ◽

Receptor Binding ◽

Cell Receptor ◽

Spike Protein ◽

Host Cell Receptor ◽

Dna Ejection ◽

Phage Dna ◽

Tail Spike

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The C-terminal domain is sufficient for host-binding activity of the Mu phage tail-spike protein

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics ◽

10.1016/j.bbapap.2010.05.003 ◽

2010 ◽

Vol 1804 (9) ◽

pp. 1738-1742 ◽

Cited By ~ 9

Author(s):

Hidetaka Suzuki ◽

Seiko Yamada ◽

Yoshiharu Toyama ◽

Shigeki Takeda

Keyword(s):

Binding Activity ◽

Spike Protein ◽

Terminal Domain ◽

Phage Tail ◽

Tail Spike

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An Engineered R-Type Pyocin Is a Highly Specific and Sensitive Bactericidal Agent for the Food-Borne Pathogen Escherichia coli O157:H7

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.01660-08 ◽

2009 ◽

Vol 53 (7) ◽

pp. 3074-3080 ◽

Cited By ~ 69

Author(s):

Dean Scholl ◽

Mike Cooley ◽

Steve R. Williams ◽

Dana Gebhart ◽

David Martin ◽

...

Keyword(s):

Escherichia Coli ◽

Antimicrobial Agents ◽

Cell Envelope ◽

Molecular Techniques ◽

Spike Protein ◽

Tail Fiber ◽

Primary Spectrum ◽

E Coli ◽

The Family ◽

Tail Spike

ABSTRACT Some strains of Pseudomonas aeruginosa produce R-type pyocins, which are high-molecular-weight phage tail-like protein complexes that have bactericidal activity against other Pseudomonas strains. These particles recognize and bind to bacterial surface structures via tail fibers, their primary spectrum determinant. R-type pyocins kill the cell by contracting a sheath-like structure and inserting their hollow core through the cell envelope, resulting in dissipation of the cellular membrane potential. We have retargeted an R-type pyocin to Escherichia coli O157:H7 by fusing a tail spike protein from an O157-specific phage, φV10, to the pyocin tail fiber. The φV10 tail spike protein recognizes and degrades the O157 lipopolysaccharide. This engineered pyocin, termed AVR2-V10, is sensitive and specific, killing 100% of diverse E. coli O157:H7 isolates but no other serotypes tested. AVR2-V10 can kill E. coli O157:H7 on beef surfaces, making it a candidate agent for the elimination of this pathogen from food products. All rare AVR2-V10-resistant mutants isolated and examined have lost the ability to produce the O157 antigen and are expected to have compromised virulence. In addition, E. coli O157:H7 exposed to and killed by AVR2-V10 do not release Shiga toxin, as is often the case with many antibiotics, suggesting potential therapeutic applications. The demonstration that a novel R-type pyocin can be created in the laboratory by fusing a catalytic tail spike from the family Podoviridae to a tail fiber of a member of the family Myoviridae is evidence that the plasticity observed among bacteriophage tail genes can, with modern molecular techniques, be exploited to produce nonnatural, targeted antimicrobial agents.

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Novel Phage-Derived Depolymerase with Activity against Proteus mirabilis Biofilms

Microorganisms ◽

10.3390/microorganisms9102172 ◽

2021 ◽

Vol 9 (10) ◽

pp. 2172

Author(s):

Cormac J. Rice ◽

Stephen A. Kelly ◽

Seamus C. O’Brien ◽

Erinn M. Melaugh ◽

Jan C. B. Ganacias ◽

...

Keyword(s):

Proteus Mirabilis ◽

Galleria Mellonella ◽

Treatment Options ◽

Pectate Lyase ◽

Bacterial Biofilm ◽

Spike Protein ◽

Resistance Development ◽

Tail Spike ◽

Tract Infections ◽

Lyase Domain

The adherence of Proteus mirabilis to the surface of urinary catheters leads to colonization and eventual blockage of the catheter lumen by unique crystalline biofilms produced by these opportunistic pathogens, making P. mirabilis one of the leading causes of catheter-associated urinary tract infections. The Proteus biofilms reduce efficiency of antibiotic-based treatment, which in turn increases the risk of antibiotic resistance development. Bacteriophages and their enzymes have recently become investigated as alternative treatment options. In this study, a novel Proteus bacteriophage (vB_PmiS_PM-CJR) was isolated from an environmental sample and fully characterized. The phage displayed depolymerase activity and the subsequent genome analysis revealed the presence of a pectate lyase domain in its tail spike protein. The protein was heterologously expressed and purified; the ability of the purified tail spike to degrade Proteus biofilms was tested. We showed that the application of the tail spike protein was able to reduce the adherence of bacterial biofilm to plastic pegs in a MBEC (minimum biofilm eradication concentration) assay and improve the survival of Galleria mellonella larvae infected with Proteus mirabilis. Our study is the first to successfully isolate and characterize a biofilm depolymerase from a Proteus phage, demonstrating the potential of this group of enzymes in treatment of Proteus infections.

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