Virion Structure and Mechanism of Genome Delivery of
Bacteriophage SU10

k 2021

Virion Structure and Mechanism of Genome Delivery of Bacteriophage SU10

ŠIBOROVÁ, Marta, Tibor FÜZIK, Michaela PROCHÁZKOVÁ, Jiří NOVÁČEK, Martin BENEŠÍK et. al.

Základní údaje

Originální název

Virion Structure and Mechanism of Genome Delivery of Bacteriophage SU10

Autoři

ŠIBOROVÁ, Marta (203 Česká republika, domácí), Tibor FÜZIK (703 Slovensko, domácí), Michaela PROCHÁZKOVÁ (203 Česká republika, domácí), Jiří NOVÁČEK (203 Česká republika, domácí), Martin BENEŠÍK (203 Česká republika, domácí), AS. NILSSON a Pavel PLEVKA (203 Česká republika, garant, domácí)

Vydání

CEITEC PhD Conference, 2021

Další údaje

Jazyk

angličtina

Typ výsledku

Prezentace na konferencích

Obor

10607 Virology

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14740/21:00123941

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

phage SU10; cryo-electron tomography

Štítky

rivok

Příznaky

Mezinárodní význam

Změněno: 24. 1. 2022 18:21, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Bacteriophages are molecular machines evolved to infect cells. Historically bacteriophages from the family Podoviridae were characterised by short non-contractile tails. Here we present the structure of native and genome releasing virion of phage SU10. SU10 has a prolate capsid with a dodecameric portal complex that features a prolonged crown-barrel. The tail of SU10 is decorated by long and short tail fibers, both present in six copies. Tail needle protrudes out from the center of the base plate. Our observations by CryoEM allows us to propose mechanism of the early stages of the phage infection. SU10 binds to the cell surface by primary and secondary receptor binding proteins. Primary receptor binding proteins, which bind reversibly, are located at distal ends of the long tail fibres. After primary receptor recognition, short tail fibres flip towards the cell surface. C-terminal receptor binding domains of short tail fibres serve as secondary irreversible receptor binding proteins. Extended nozzle is formed by a remodeled tail complex together with flipped short tail fibres. During attachment of secondary receptor binding proteins the tail needle mechanically disrupts the outer cell membrane and dissociates from the virion. Phage core proteins are ejected from the capsid and form a translocation channel. Transglycosylase domains, which are located on the outer surface of the translocation channel, hydrolytically degrade the cell wall. Translocation channel together with extended nozzle serve as a tunnel for phage DNA delivery into the bacterial cytoplasm. Our study reveals major structural changes of podovirus tail upon phage attachment on the cell surface were not observed up to date.

Návaznosti

LL1906, projekt VaV

Název: Replikace fágů v bakteriálním biofilmu

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

Citovat

ŠIBOROVÁ, Marta, Tibor FÜZIK, Michaela PROCHÁZKOVÁ, Jiří NOVÁČEK, Martin BENEŠÍK, AS. NILSSON a Pavel PLEVKA. Virion Structure and Mechanism of Genome Delivery of Bacteriophage SU10. In CEITEC PhD Conference. 2021.

@proceedings{1826557,
   author = {Šiborová, Marta and Füzik, Tibor and Procházková, Michaela and Nováček, Jiří and Benešík, Martin and Nilsson, AS. and Plevka, Pavel},
   booktitle = {CEITEC PhD Conference},
   keywords = {phage SU10; cryo-electron tomography},
   language = {eng},
   title = {Virion Structure and Mechanism of Genome Delivery of Bacteriophage SU10},
   url = {https://www.ceitec.eu/ceitec-phd-conference-2021/a3988},
   year = {2021}
}

TY  - CONF
ID  - 1826557
AU  - Šiborová, Marta - Füzik, Tibor - Procházková, Michaela - Nováček, Jiří - Benešík, Martin - Nilsson, AS. - Plevka, Pavel
PY  - 2021
TI  - Virion Structure and Mechanism of Genome Delivery of Bacteriophage SU10
KW  - phage SU10
KW  - cryo-electron tomography
UR  - https://www.ceitec.eu/ceitec-phd-conference-2021/a3988
N2  - Bacteriophages are molecular machines evolved to infect cells. Historically bacteriophages from the family Podoviridae were characterised by short non-contractile tails. Here we present the structure of native and genome releasing virion of phage SU10. SU10 has a prolate capsid with a dodecameric portal complex that features a prolonged crown-barrel. The tail of SU10 is decorated by long and short tail fibers, both present in six copies. Tail needle protrudes out from the center of the base plate. Our observations by CryoEM allows us to propose mechanism of the early stages of the phage infection. SU10 binds to the cell surface by primary and secondary receptor binding proteins. Primary receptor binding proteins, which bind reversibly, are located at distal ends of the long tail fibres. After primary receptor recognition, short tail fibres flip towards the cell surface. C-terminal receptor binding domains of short tail fibres serve as secondary irreversible receptor binding proteins. Extended nozzle is formed by a remodeled tail complex together with flipped short tail fibres. During attachment of secondary receptor binding proteins the tail needle mechanically disrupts the outer cell membrane and dissociates from the virion. Phage core proteins are ejected from the capsid and form a translocation channel. Transglycosylase domains, which are located on the outer surface of the translocation channel, hydrolytically degrade the cell wall. Translocation channel together with extended nozzle serve as a tunnel for phage DNA delivery into the bacterial cytoplasm. Our study reveals major structural changes of podovirus tail upon phage attachment on the cell surface were not observed up to date.
ER  -

Podrobný výpis o publikaci