Mechanism of the long tail-fiber deployment of bacteriophages T-even and its role in adsorption, infection and sedimentation

The Yersinia bacteriophages fPS-2, fPS-65, and fPS-90, isolated from pig stools, have long contractile tails and elongated heads, and they belong to genus Tequatroviruses in the order Caudovirales. The phages exhibited relatively wide host ranges among Yersinia pseudotuberculosis and related species. One-step growth curve experiments revealed that the phages have latent periods of 50–80 min with burst sizes of 44–65 virions per infected cell. The phage genomes consist of circularly permuted dsDNA of 169,060, 167,058, and 167,132 bp in size, respectively, with a G + C content 35.3%. The number of predicted genes range from 267 to 271. The phage genomes are 84–92% identical to each other and ca 85% identical to phage T4. The phage receptors were identified by whole genome sequencing of spontaneous phage-resistant mutants. The phage-resistant strains had mutations in the ompF, galU, hldD, or hldE genes. OmpF is a porin, and the other genes encode lipopolysaccharide (LPS) biosynthetic enzymes. The ompF, galU, and hldE mutants were successfully complemented in trans with respective wild-type genes. The host recognition was assigned to long tail fiber tip protein Gp38, analogous to that of T-even phages such as Salmonella phage S16, specifically to the distal β-helices connecting loops.

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Structure of two phages of Bacillus thuringiensis and B. cereus

Canadian Journal of Microbiology ◽

10.1139/m74-005 ◽

1974 ◽

Vol 20 (1) ◽

pp. 29-33 ◽

Cited By ~ 2

Author(s):

H.-W. Ackermann ◽

W. A. Smirnoff ◽

A. Z. Bilsky

Keyword(s):

Bacillus Thuringiensis ◽

Uranyl Acetate ◽

Tail Fiber ◽

Long Tail ◽

Different Dimensions

Phage TP50 resembles phage SP50 of B. subtilis and phage No. 1 of B. mycoides. Phage PBC1 has a long tail fiber like flagella-specific phages and resembles B. pumilus phage PBP1. The latter was reexamined but has different dimensions. Heads of phages TP50 and PBP1 are icosahedral. Staining with uranyl acetate causes shrinkage of phage heads. Lysates of B. cereus contain cubic, round, or filamentous particles not previously described.

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Bacteriophage T4 long tail fiber domains

Biophysical Reviews ◽

10.1007/s12551-017-0348-5 ◽

2017 ◽

Vol 10 (2) ◽

pp. 463-471 ◽

Cited By ~ 12

Author(s):

Paul Hyman ◽

Mark van Raaij

Keyword(s):

Bacteriophage T4 ◽

Tail Fiber ◽

Long Tail

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Molecular anatomy of the receptor binding module of a bacteriophage long tail fiber

PLoS Pathogens ◽

10.1371/journal.ppat.1008193 ◽

2019 ◽

Vol 15 (12) ◽

pp. e1008193 ◽

Cited By ~ 3

Author(s):

Mohammad Z. Islam ◽

Andrei Fokine ◽

Marthandan Mahalingam ◽

Zhihong Zhang ◽

Carmela Garcia-Doval ◽

...

Keyword(s):

Receptor Binding ◽

Tail Fiber ◽

Long Tail ◽

Molecular Anatomy

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A component of the side tail fiber of Escherichia coli bacteriophage lambda can functionally replace the receptor-recognizing part of a long tail fiber protein of the unrelated bacteriophage T4.

Journal of Bacteriology ◽

10.1128/jb.171.8.4378-4384.1989 ◽

1989 ◽

Vol 171 (8) ◽

pp. 4378-4384 ◽

Cited By ~ 29

Author(s):

D Montag ◽

H Schwarz ◽

U Henning

Keyword(s):

Escherichia Coli ◽

Bacteriophage Lambda ◽

Bacteriophage T4 ◽

Tail Fiber ◽

Tail Fiber Protein ◽

Long Tail ◽

Fiber Protein

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

Viruses ◽

10.3390/v9070168 ◽

2017 ◽

Vol 9 (7) ◽

pp. 168 ◽

Cited By ~ 16

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

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Evaluating Phage Tail Fiber Receptor-Binding Proteins Using a Luminescent Flow-Through 96-Well Plate Assay

Frontiers in Microbiology ◽

10.3389/fmicb.2021.741304 ◽

2021 ◽

Vol 12 ◽

Author(s):

Emma L. Farquharson ◽

Ashlyn Lightbown ◽

Elsi Pulkkinen ◽

Téa Russell ◽

Brenda Werner ◽

...

Keyword(s):

Escherichia Coli ◽

Host Range ◽

Infection Process ◽

Bacterial Disease ◽

Tail Fiber ◽

Long Tail ◽

Bacterial Surface ◽

Specific Phage ◽

Phage Tail ◽

Tail Fibers

Phages have demonstrated significant potential as therapeutics in bacterial disease control and as diagnostics due to their targeted bacterial host range. Host range has typically been defined by plaque assays; an important technique for therapeutic development that relies on the ability of a phage to form a plaque upon a lawn of monoculture bacteria. Plaque assays cannot be used to evaluate a phage’s ability to recognize and adsorb to a bacterial strain of interest if the infection process is thwarted post-adsorption or is temporally delayed, and it cannot highlight which phages have the strongest adsorption characteristics. Other techniques, such as classic adsorption assays, are required to define a phage’s “adsorptive host range.” The issue shared amongst all adsorption assays, however, is that they rely on the use of a complete bacteriophage and thus inherently describe when all adsorption-specific machinery is working together to facilitate bacterial surface adsorption. These techniques cannot be used to examine individual interactions between a singular set of a phage’s adsorptive machinery (like long tail fibers, short tail fibers, tail spikes, etc.) and that protein’s targeted bacterial surface receptor. To address this gap in knowledge we have developed a high-throughput, filtration-based, bacterial binding assay that can evaluate the adsorptive capability of an individual set of a phage’s adsorption machinery. In this manuscript, we used a fusion protein comprised of an N-terminal bioluminescent tag translationally fused to T4’s long tail fiber binding tip (gp37) to evaluate and quantify gp37’s relative adsorptive strength against the Escherichia coli reference collection (ECOR) panel of 72 Escherichia coli isolates. Gp37 could adsorb to 61 of the 72 ECOR strains (85%) but coliphage T4 only formed plaques on 8 of the 72 strains (11%). Overlaying these two datasets, we were able to identify ECOR strains incompatible with T4 due to failed adsorption, and strains T4 can adsorb to but is thwarted in replication at a step post-adsorption. While this manuscript only demonstrates our assay’s ability to characterize adsorptive capabilities of phage tail fibers, our assay could feasibly be modified to evaluate other adsorption-specific phage proteins.

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