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.

Podrobný výpis o publikaci