ŠIBOROVÁ, Marta, Tibor FÜZIK, Michaela PROCHÁZKOVÁ, Jiří NOVÁČEK, Martin BENEŠÍK, AS. NILSSON and Pavel PLEVKA. Virion Structure and Mechanism of Genome Delivery of Bacteriophage SU10. In CEITEC PhD Conference. 2021.
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Basic information
Original name Virion Structure and Mechanism of Genome Delivery of Bacteriophage SU10
Authors ŠIBOROVÁ, Marta (203 Czech Republic, belonging to the institution), Tibor FÜZIK (703 Slovakia, belonging to the institution), Michaela PROCHÁZKOVÁ (203 Czech Republic, belonging to the institution), Jiří NOVÁČEK (203 Czech Republic, belonging to the institution), Martin BENEŠÍK (203 Czech Republic, belonging to the institution), AS. NILSSON and Pavel PLEVKA (203 Czech Republic, guarantor, belonging to the institution).
Edition CEITEC PhD Conference, 2021.
Other information
Original language English
Type of outcome Presentations at conferences
Field of Study 10607 Virology
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
WWW URL
RIV identification code RIV/00216224:14740/21:00123941
Organization unit Central European Institute of Technology
Keywords in English phage SU10; cryo-electron tomography
Tags rivok
Tags International impact
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 24/1/2022 18:21.
Abstract
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.
Links
LL1906, research and development projectName: Replikace fágů v bakteriálním biofilmu
Investor: Ministry of Education, Youth and Sports of the CR, Phage replication in bacterial biofilm
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