A hunting strategy and virion structure of P. aeruginosa
bacteriophage JBD30 revealed by cryo-electron microscopy

a 2022

A hunting strategy and virion structure of P. aeruginosa bacteriophage JBD30 revealed by cryo-electron microscopy

VALENTOVÁ, Lucie, Tibor FÜZIK a Pavel PLEVKA

Základní údaje

Originální název

A hunting strategy and virion structure of P. aeruginosa bacteriophage JBD30 revealed by cryo-electron microscopy

Autoři

VALENTOVÁ, Lucie (203 Česká republika, domácí), Tibor FÜZIK (703 Slovensko, domácí) a Pavel PLEVKA (203 Česká republika, garant, domácí)

Vydání

The XVIII Discussions in Structural Molecular Biology and the 5th User Meeting of CIISB, 2022

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10607 Virology

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14740/22:00126452

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

Pseudomonas aeruginosa; bacteriophage JBD30; structure; replication strategy; cryo-electron microscopy

Štítky

CF CRYO, rivok

Příznaky

Mezinárodní význam

Změněno: 12. 2. 2023 19:39, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Pseudomonas aeruginosa is a human pathogen, whose treatment is complicated by its frequent antibiotic-resistance. Siphoviridae bacteriophage JBD30 infects and kills bacterium P. aeruginosa, which makes it a potential agent for phage therapy. Here we present the structure of bacteriophage JBD30 virion and its replication strategy, revealed by the combination of cryo-electron microscopy analysis techniques and cryo-electron tomography. The virion of bacteriophage JBD30 is composed of non-enveloped icosahedral capsid, long flexible non-contractile tail and baseplate decorated with tail fibers. The capsid with a diameter of 60 nm is built from major capsid protein organised in T = 7 icosahedral lattice and decorated on three-fold and pseudo-threefold axis with trimers of minor capsid protein. In one vertex of the capsid, the penton of major capsid protein is replaced by dodecameric portal. The portal complex forms an interface between the capsid and 180 nm long tail. The tail is built from 44 hexameric discs of major tail protein. Distal tail protein trimer follows-up the last tail disc and forms an attachment site for the long tail fibers. The baseplate is terminated with a tripod complex of receptor binding protein trimers. Using cryo-electron tomography we followed the infection process of P. aeruginosa by JBD30 phage from attachment to bacterial cell, to the production of new phage progeny and host cell lysis. Bacteriophage JBD30 uses its long tail fibres for binding to P. aeruginosa pili type IV. After attachment to pili, the virion either diffuses or is pulled towards the cellular surface, where it irreversibly binds by its receptor binding proteins. Afterwards, the phage punctures the outer cellular membrane, degrades the peptidoglycan layer and injects its DNA into host cell. New phage progeny is released approximately after 80 minutes post infection. The combination of cryo-electron microscopy methods allowed us, to propose the mechanism of key stages of phage infection and describe it at molecular level.

Návaznosti

LL1906, projekt VaV

Název: Replikace fágů v bakteriálním biofilmu

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Replikace fágů v bakteriálním biofilmu

Citovat

VALENTOVÁ, Lucie, Tibor FÜZIK a Pavel PLEVKA. A hunting strategy and virion structure of P. aeruginosa bacteriophage JBD30 revealed by cryo-electron microscopy. In The XVIII Discussions in Structural Molecular Biology and the 5th User Meeting of CIISB. 2022.

@proceedings{2211951,
   author = {Valentová, Lucie and Füzik, Tibor and Plevka, Pavel},
   booktitle = {The XVIII Discussions in Structural Molecular Biology and the 5th User Meeting of CIISB},
   keywords = {Pseudomonas aeruginosa; bacteriophage JBD30; structure; replication strategy; cryo-electron microscopy},
   language = {eng},
   title = {A hunting strategy and virion structure of P. aeruginosa bacteriophage JBD30 revealed by cryo-electron microscopy},
   url = {https://www.xray.cz/setkani/abst2022/406.htm},
   year = {2022}
}

TY  - CONF
ID  - 2211951
AU  - Valentová, Lucie - Füzik, Tibor - Plevka, Pavel
PY  - 2022
TI  - A hunting strategy and virion structure of P. aeruginosa bacteriophage JBD30 revealed by cryo-electron microscopy
KW  - Pseudomonas aeruginosa
KW  - bacteriophage JBD30
KW  - structure
KW  - replication strategy
KW  - cryo-electron microscopy
UR  - https://www.xray.cz/setkani/abst2022/406.htm
N2  - Pseudomonas aeruginosa is a human pathogen, whose treatment is complicated by its frequent antibiotic-resistance. Siphoviridae bacteriophage JBD30 infects and kills bacterium P. aeruginosa, which makes it a potential agent for phage therapy. Here we present the structure of bacteriophage JBD30 virion and its replication strategy, revealed by the combination of cryo-electron microscopy analysis techniques and cryo-electron tomography. The virion of bacteriophage JBD30 is composed of non-enveloped icosahedral capsid, long flexible non-contractile tail and baseplate decorated with tail fibers. The capsid with a diameter of 60 nm is built from major capsid protein organised in T = 7 icosahedral lattice and decorated on three-fold and pseudo-threefold axis with trimers of minor capsid protein. In one vertex of the capsid, the penton of major capsid protein is replaced by dodecameric portal. The portal complex forms an interface between the capsid and 180 nm long tail. The tail is built from 44 hexameric discs of major tail protein. Distal tail protein trimer follows-up the last tail disc and forms an attachment site for the long tail fibers. The baseplate is terminated with a tripod complex of receptor binding protein trimers. Using cryo-electron tomography we followed the infection process of P. aeruginosa by JBD30 phage from attachment to bacterial cell, to the production of new phage progeny and host cell lysis. Bacteriophage JBD30 uses its long tail fibres for binding to P. aeruginosa pili type IV. After attachment to pili, the virion either diffuses or is pulled towards the cellular surface, where it irreversibly binds by its receptor binding proteins. Afterwards, the phage punctures the outer cellular membrane, degrades the peptidoglycan layer and injects its DNA into host cell. New phage progeny is released approximately after 80 minutes post infection. The combination of cryo-electron microscopy methods allowed us, to propose the mechanism of key stages of phage infection and describe it at molecular level.
ER  -

VALENTOVÁ, Lucie, Tibor FÜZIK a Pavel PLEVKA. A hunting strategy and virion structure of P. aeruginosa bacteriophage JBD30 revealed by cryo-electron microscopy. In \textit{The XVIII Discussions in Structural Molecular Biology and the 5th User Meeting of CIISB}. 2022.

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