Baseplate structure of bacteriophage phi812 and mechanism of
cell binding and degradation

a 2021

Baseplate structure of bacteriophage phi812 and mechanism of cell binding and degradation

BÍŇOVSKÝ, Ján; Marta ŠIBOROVÁ; Jiří NOVÁČEK; M. VAN RAAIJ; Pavel PLEVKA et. al.

Základní údaje

Originální název

Baseplate structure of bacteriophage phi812 and mechanism of cell binding and degradation

Autoři

BÍŇOVSKÝ, Ján (703 Slovensko, domácí); Marta ŠIBOROVÁ (203 Česká republika, domácí); Jiří NOVÁČEK (203 Česká republika, domácí); M. VAN RAAIJ a Pavel PLEVKA (203 Česká republika, garant, domácí)

Vydání

Phage/Virus Assembly 2021, 2021

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10607 Virology

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14740/21:00123931

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

Staphylococcus aureus; Bacteriophage; Myoviridae

Štítky

rivok

Změněno: 24. 1. 2022 15:32, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Antibiotic-resistant strains of Staphylococcus aureus cause human infections that are difficult to treat and can lead to death . Bacteriophage (phage) phi812K1/420 from the family Myoviridae infects 95% of S. aureus isolates and therefore is a promising candidate for a phage therapy agent . As the native phage particle approaches its host cell, phage receptor-binding proteins make a contact with the host cell wall. This interaction triggers a cascade of structural changes in the baseplate, resulting in phage tail contraction and genome ejection . Mechanistic description of the baseplate re-organization, however, remains unknown. Using cryo-electron microscopy (cryo-EM), we reconstructed the phage baseplate in native and contracted states. The reconstruction of the center of native baseplate reaches resolution of 4 Å, which enables us to build individual protein structures. Also, selected proteins involved in host cell wall binding and penetration were produced in recombinant form and their structures were solved using X-ray crystallography and cryo-EM single-particle reconstruction. The protein structures will be fitted into reconstruction of the contracted baseplate. Our results provide first structural characterisation of contractile phage infecting a Gram-positive bacterium. Comparison of the two distinct baseplate states will allow us to describe molecular mechanism of initial stage of phage infection in detail.

Návaznosti

LL1906, projekt VaV

Název: Replikace fágů v bakteriálním biofilmu

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

Citovat

BÍŇOVSKÝ, Ján; Marta ŠIBOROVÁ; Jiří NOVÁČEK; M. VAN RAAIJ a Pavel PLEVKA. Baseplate structure of bacteriophage phi812 and mechanism of cell binding and degradation. In Phage/Virus Assembly 2021. 2021.

@proceedings{1826480,
   author = {Bíňovský, Ján and Šiborová, Marta and Nováček, Jiří and Van Raaij, M. and Plevka, Pavel},
   booktitle = {Phage/Virus Assembly 2021},
   keywords = {Staphylococcus aureus; Bacteriophage; Myoviridae},
   language = {eng},
   title = {Baseplate structure of bacteriophage phi812 and mechanism of cell binding and degradation},
   url = {https://pvaconference.wixsite.com/pva2021},
   year = {2021}
}

TY  - CONF
ID  - 1826480
AU  - Bíňovský, Ján - Šiborová, Marta - Nováček, Jiří - Van Raaij, M. - Plevka, Pavel
PY  - 2021
TI  - Baseplate structure of bacteriophage phi812 and mechanism of cell binding and degradation
KW  - Staphylococcus aureus
KW  - Bacteriophage
KW  - Myoviridae
UR  - https://pvaconference.wixsite.com/pva2021
N2  - Antibiotic-resistant strains of Staphylococcus aureus cause human infections that are difficult to treat and can lead to death . Bacteriophage (phage) phi812K1/420 from the family Myoviridae infects 95% of S. aureus isolates and therefore is a promising candidate for a phage therapy agent . As the native phage particle approaches its host cell, phage receptor-binding proteins make a contact with the host cell wall. This interaction triggers a cascade of structural changes in the baseplate, resulting in phage tail contraction and genome ejection . Mechanistic description of the baseplate re-organization, however, remains unknown. Using cryo-electron microscopy (cryo-EM), we reconstructed the phage baseplate in native and contracted states. The reconstruction of the center of native baseplate reaches resolution of 4 Å, which enables us to build individual protein structures. Also, selected proteins involved in host cell wall binding and penetration were produced in recombinant form and their structures were solved using X-ray crystallography and cryo-EM single-particle reconstruction. The protein structures will be fitted into reconstruction of the contracted baseplate. Our results provide first structural characterisation of contractile phage infecting a Gram-positive bacterium. Comparison of the two distinct baseplate states will allow us to describe molecular mechanism of initial stage of phage infection in detail.
ER  -

BÍŇOVSKÝ, Ján; Marta ŠIBOROVÁ; Jiří NOVÁČEK; M. VAN RAAIJ a Pavel PLEVKA. Baseplate structure of bacteriophage phi812 and mechanism of cell binding and degradation. In \textit{Phage/Virus Assembly 2021}. 2021.

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