Structural basis for the multitasking nature of the potato
virus Y coat protein

J 2019

Structural basis for the multitasking nature of the potato virus Y coat protein

KEZAR, A., L. KAVCIC, Martin POLÁK, Jiří NOVÁČEK, I. GUTIERREZ-AGUIRRE et. al.

Basic information

Original name

Structural basis for the multitasking nature of the potato virus Y coat protein

Authors

KEZAR, A., L. KAVCIC, Martin POLÁK (203 Czech Republic, belonging to the institution), Jiří NOVÁČEK (203 Czech Republic, guarantor, belonging to the institution), I. GUTIERREZ-AGUIRRE, M.T. ZNIDARIC, A. CO, K. STARE, K. GRUDEN, M. RAVNIKAR, D. PAHOVNIK, E. ZAGAR, F. MERZEL, G. ANDERLUH and M. PODOBNIK

Edition

Science advances, New York, American Association for the Advancement of Science, 2019, 2375-2548

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 13.117

RIV identification code

RIV/00216224:14740/19:00113326

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1126/sciadv.aaw3808

UT WoS

000478770400067

Keywords in English

REAL-TIME PCR; CRYO-EM; PLANT-VIRUSES; POTYVIRUS; TERMINUS; ELECTROSTATICS; REFINEMENT; RESOLUTION; RESIDUES; PVYNTN

Abstract

V originále

Potato virus Y (PVY) is among the most economically important plant pathogens. Using cryoelectron microscopy, we determined the near-atomic structure of PVY's flexuous virions, revealing a previously unknown lumenal interplay between extended carboxyl-terminal regions of the coat protein units and viral RNA. RNA-coat protein interactions are crucial for the helical configuration and stability of the virion, as revealed by the unique near-atomic structure of RNA-free virus-like particles. The structures offer the first evidence for plasticity of the coat protein's amino- and carboxyl-terminal regions. Together with mutational analysis and in planta experiments, we show their crucial role in PVY infectivity and explain the ability of the coat protein to perform multiple biological tasks. Moreover, the high modularity of PVY virus-like particles suggests their potential as a new molecular scaffold for nanobiotechnological applications.

Links

LM2015043, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR

90043, large research infrastructures

Name: CIISB

Citovat

KEZAR, A., L. KAVCIC, Martin POLÁK, Jiří NOVÁČEK, I. GUTIERREZ-AGUIRRE, M.T. ZNIDARIC, A. CO, K. STARE, K. GRUDEN, M. RAVNIKAR, D. PAHOVNIK, E. ZAGAR, F. MERZEL, G. ANDERLUH and M. PODOBNIK. Structural basis for the multitasking nature of the potato virus Y coat protein. Science advances. New York: American Association for the Advancement of Science, 2019, vol. 5, No 7, p. 1-13. ISSN 2375-2548. Available from: https://dx.doi.org/10.1126/sciadv.aaw3808.

@article{1637362,
   author = {Kezar, A. and Kavcic, L. and Polák, Martin and Nováček, Jiří and GutierrezandAguirre, I. and Znidaric, M.T. and Co, A. and Stare, K. and Gruden, K. and Ravnikar, M. and Pahovnik, D. and Zagar, E. and Merzel, F. and Anderluh, G. and Podobnik, M.},
   article_location = {New York},
   article_number = {7},
   doi = {http://dx.doi.org/10.1126/sciadv.aaw3808},
   keywords = {REAL-TIME PCR; CRYO-EM; PLANT-VIRUSES; POTYVIRUS; TERMINUS; ELECTROSTATICS; REFINEMENT; RESOLUTION; RESIDUES; PVYNTN},
   language = {eng},
   issn = {2375-2548},
   journal = {Science advances},
   title = {Structural basis for the multitasking nature of the potato virus Y coat protein},
   url = {https://advances.sciencemag.org/content/advances/5/7/eaaw3808.full.pdf},
   volume = {5},
   year = {2019}
}

TY  - JOUR
ID  - 1637362
AU  - Kezar, A. - Kavcic, L. - Polák, Martin - Nováček, Jiří - Gutierrez-Aguirre, I. - Znidaric, M.T. - Co, A. - Stare, K. - Gruden, K. - Ravnikar, M. - Pahovnik, D. - Zagar, E. - Merzel, F. - Anderluh, G. - Podobnik, M.
PY  - 2019
TI  - Structural basis for the multitasking nature of the potato virus Y coat protein
JF  - Science advances
VL  - 5
IS  - 7
SP  - 1-13
EP  - 1-13
PB  - American Association for the Advancement of Science
SN  - 23752548
KW  - REAL-TIME PCR
KW  - CRYO-EM
KW  - PLANT-VIRUSES
KW  - POTYVIRUS
KW  - TERMINUS
KW  - ELECTROSTATICS
KW  - REFINEMENT
KW  - RESOLUTION
KW  - RESIDUES
KW  - PVYNTN
UR  - https://advances.sciencemag.org/content/advances/5/7/eaaw3808.full.pdf
L2  - https://advances.sciencemag.org/content/advances/5/7/eaaw3808.full.pdf
N2  - Potato virus Y (PVY) is among the most economically important plant pathogens. Using cryoelectron microscopy, we determined the near-atomic structure of PVY's flexuous virions, revealing a previously unknown lumenal interplay between extended carboxyl-terminal regions of the coat protein units and viral RNA. RNA-coat protein interactions are crucial for the helical configuration and stability of the virion, as revealed by the unique near-atomic structure of RNA-free virus-like particles. The structures offer the first evidence for plasticity of the coat protein's amino- and carboxyl-terminal regions. Together with mutational analysis and in planta experiments, we show their crucial role in PVY infectivity and explain the ability of the coat protein to perform multiple biological tasks. Moreover, the high modularity of PVY virus-like particles suggests their potential as a new molecular scaffold for nanobiotechnological applications.
ER  -

KEZAR, A., L. KAVCIC, Martin POLÁK, Jiří NOVÁČEK, I. GUTIERREZ-AGUIRRE, M.T. ZNIDARIC, A. CO, K. STARE, K. GRUDEN, M. RAVNIKAR, D. PAHOVNIK, E. ZAGAR, F. MERZEL, G. ANDERLUH and M. PODOBNIK. Structural basis for the multitasking nature of the potato virus Y coat protein. \textit{Science advances}. New York: American Association for the Advancement of Science, 2019, vol.~5, No~7, p.~1-13. ISSN~2375-2548. Available from: https://dx.doi.org/10.1126/sciadv.aaw3808.

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