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

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

Biophysical Chemistry ◽

10.1016/0301-4622(95)00117-4 ◽

1996 ◽

Vol 59 (1-2) ◽

pp. 41-59 ◽

Cited By ~ 11

Author(s):

E. Kellenberger ◽

E. Stauffer ◽

M. Häner ◽

A. Lustig ◽

D. Karamata

Keyword(s):

Tail Fiber ◽

Long Tail

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Specific Detection of Yersinia pestis Based on Receptor Binding Proteins of Phages

Pathogens ◽

10.3390/pathogens9080611 ◽

2020 ◽

Vol 9 (8) ◽

pp. 611 ◽

Cited By ~ 1

Author(s):

Friederike Born ◽

Peter Braun ◽

Holger C. Scholz ◽

Gregor Grass

Keyword(s):

Yersinia Pestis ◽

Receptor Binding ◽

Fluorescent Proteins ◽

Diagnostic Methods ◽

Tail Fiber ◽

Yersinia Species ◽

Recombinant Receptor ◽

F1 Antigen ◽

Phage Receptor ◽

Bacterial Plaque

The highly pathogenic bacterium Yersinia pestis is the causative agent of plague, a notorious infectious zoonotic disease. When transmitted from person to person as pneumonic plague via droplets, Y. pestis is highly contagious and in most cases is fatal if left untreated. Thus, when plague is suspected, rapid diagnosis is crucial, as a serious course of the infection is only averted by early antibiotic therapy. The bacterium is easy to cultivate, accessible and has a high potential for nefarious use such as bioterrorism. Highly specific, rapid and easy-to-use confirmatory diagnostic methods are required to reliably identify the pathogen independently from PCR-based methods or F1 antigen-based immunological detection. Yersinia pestis specific phages such as L-413C and ΦA1122 are already used for detection of Y. pestis in bacterial plaque or biosensor assays. Here, we made use of the host specificities conferred by phage receptor binding (or tail fiber/spike) proteins (RBP) for developing a specific, fast and simple fluorescence-microscopy-based detection method for Y. pestis. Genes of putative RBP of phages L-413C (gpH) and ΦA1122 (gp17) were fused with those of fluorescent proteins and recombinant receptor-reporter fusion proteins were produced heterologously in Escherichia coli. When first tested on attenuated Y. pestis strain EV76, RBP-reporters bound to the bacterial cell surface. This assay could be completed within a few minutes using live or formaldehyde-inactivated cells. Specificity tests using cultures of closely related Yersinia species and several inactivated fully virulent Y. pestis strains exhibited high specificities of the RBP-reporters against Y. pestis. The L-413C RBP proved to be especially specific, as it only detected Y. pestis at all temperatures tested, whereas the RBP of ΦA1122 also bound to Y. pseudotuberculosis strains at 37 °C (but not at 28, 20 or 6 °C). Finally, the Y. pestis-specific capsule, produced when grown at 37 °C, significantly reduced binding of phage ΦA1122 RBP, whereas the capsule only slightly diminished binding of L-413C RBP.

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