Baseplate structure of bacteriophage phi812 reveals functions
of host cell recognition and cell wall degradation

a 2021

Baseplate structure of bacteriophage phi812 reveals functions of host cell recognition and cell wall degradation

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

Základní údaje

Originální název

Baseplate structure of bacteriophage phi812 reveals functions of host cell recognition and cell wall 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

CEITEC PhD Conference 2021, 2021

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/00216224:14740/21:00123924

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

Staphylococcus aureus; Bacteriophage; Myoviridae

Štítky

rivok

Změněno: 24. 1. 2022 18:35, 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 has been found to infect 95% of tested S. aureus strains and therefore is considered as a potential phage therapy agent. As the native phage particle approaches its host cell, primary phage receptors make a contact with the host cell wall. This interaction triggers cascade of structural changes in the baseplate, resulting in phage tail contraction and genome delivery. Mechanistic description of the baseplate re-organization, however, remains unknown. Using cryo-electron microscopy (cryo-EM), we reconstructed the phage baseplate before and after the attachment to host cell. Moreover, we performed cryo-EM single-particle analysis of recombinant tail spike protein (TSP). Dislocation of the TSP from the center of native phage baseplate suggests that it may play a role in triggering the whole contraction mechanism. The structures of the baseplate were reconstructed in resolution of 3.5-5 Å and we are in process of building individual protein structures. We have already solved the structure of the C-terminal domain of TSP with putative glycerol-diesterase activity, which sticks out from the phage baseplate. Such orientation suggests that the TSP can readily degrade host call wall upon phage attachment, making way for tail tube insertion. We assume that as the TSP C-terminal domain is drawn towards the cell wall, the N-terminal domain detaches from phage baseplate, causing instability and consequent baseplate re-organization.

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 reveals functions of host cell recognition and cell wall degradation. In CEITEC PhD Conference 2021. 2021.

@proceedings{1826277,
   author = {Bíňovský, Ján and Šiborová, Marta and Nováček, Jiří and Van Raaij, M. and Plevka, Pavel},
   booktitle = {CEITEC PhD Conference 2021},
   keywords = {Staphylococcus aureus; Bacteriophage; Myoviridae},
   language = {eng},
   title = {Baseplate structure of bacteriophage phi812 reveals functions of host cell recognition and cell wall degradation},
   url = {https://www.ceitec.eu/ceitec-phd-conference-2021/a3988},
   year = {2021}
}

TY  - CONF
ID  - 1826277
AU  - Bíňovský, Ján - Šiborová, Marta - Nováček, Jiří - Van Raaij, M. - Plevka, Pavel
PY  - 2021
TI  - Baseplate structure of bacteriophage phi812 reveals functions of host cell recognition and cell wall degradation
KW  - Staphylococcus aureus
KW  - Bacteriophage
KW  - Myoviridae
UR  - https://www.ceitec.eu/ceitec-phd-conference-2021/a3988
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 has been found to infect 95% of tested S. aureus strains and therefore is considered as a potential phage therapy agent. As the native phage particle approaches its host cell, primary phage receptors make a contact with the host cell wall. This interaction triggers cascade of structural changes in the baseplate, resulting in phage tail contraction and genome delivery. Mechanistic description of the baseplate re-organization, however, remains unknown. Using cryo-electron microscopy (cryo-EM), we reconstructed the phage baseplate before and after the attachment to host cell. Moreover, we performed cryo-EM single-particle analysis of recombinant tail spike protein (TSP). Dislocation of the TSP from the center of native phage baseplate suggests that it may play a role in triggering the whole contraction mechanism. The structures of the baseplate were reconstructed in resolution of 3.5-5 Å and we are in process of building individual protein structures. We have already solved the structure of the C-terminal domain of TSP with putative glycerol-diesterase activity, which sticks out from the phage baseplate. Such orientation suggests that the TSP can readily degrade host call wall upon phage attachment, making way for tail tube insertion. We assume that as the TSP C-terminal domain is drawn towards the cell wall, the N-terminal domain detaches from phage baseplate, causing instability and consequent baseplate re-organization.
ER  -

Podrobný výpis o publikaci