Structure and Genome Release Mechanism of the Human Cardiovirus
Saffold Virus 3

J 2016

Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3

MULLAPUDI, Edukondalu; Jiří NOVÁČEK; Lenka PÁLKOVÁ; Pavel KULICH; A. Michael LINDBERG et al.

Základní údaje

Originální název

Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3

Autoři

MULLAPUDI, Edukondalu; Jiří NOVÁČEK; Lenka PÁLKOVÁ; Pavel KULICH; A. Michael LINDBERG; Frank J. M. VAN KUPPEVELD a Pavel PLEVKA

Vydání

JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2016, 0022-538X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.663

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/16:00093713

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

HUMAN ENTEROVIRUS 71; COMMON COLD VIRUS; CRYOELECTRON MICROSCOPY; 3-DIMENSIONAL STRUCTURE; HUMAN RHINOVIRUS-2; CELLULAR RECEPTOR; THEILER VIRUS; POLIOVIRUS; PICORNAVIRUS; BINDING

Štítky

rivok

Změněno: 27. 2. 2017 10:51, Mgr. Eva Špillingová

Anotace

V originále

In order to initiate an infection, viruses need to deliver their genomes into cells. This involves uncoating the genome and transporting it to the cytoplasm. The process of genome delivery is not well understood for nonenveloped viruses. We address this gap in our current knowledge by studying the uncoating of the nonenveloped human cardiovirus Saffold virus 3 (SAFV-3) of the family Picornaviridae. SAFVs cause diseases ranging from gastrointestinal disorders to meningitis. We present a structure of a native SAFV-3 virion determined to 2.5 angstrom by X-ray crystallography and an 11-angstrom-resolution cryo-electron microscopy reconstruction of an "altered" particle that is primed for genome release. The altered particles are expanded relative to the native virus and contain pores in the capsid that might serve as channels for the release of VP4 subunits, N termini of VP1, and the RNA genome. Unlike in the related enteroviruses, pores in SAFV-3 are located roughly between the icosahedral 3- and 5-fold axes at an interface formed by two VP1 and one VP3 subunit. Furthermore, in native conditions many cardioviruses contain a disulfide bond formed by cysteines that are separated by just one residue. The disulfide bond is located in a surface loop of VP3. We determined the structure of the SAFV-3 virion in which the disulfide bonds are reduced. Disruption of the bond had minimal effect on the structure of the loop, but it increased the stability and decreased the infectivity of the virus. Therefore, compounds specifically disrupting or binding to the disulfide bond might limit SAFV infection. IMPORTANCE A capsid assembled from viral proteins protects the virus genome during transmission from one cell to another. However, when a virus enters a cell the virus genome has to be released from the capsid in order to initiate infection. This process is not well understood for nonenveloped viruses. We address this gap in our current knowledge by studying the genome release of Human Saffold virus 3. Saffold viruses cause diseases ranging from gastrointestinal disorders to meningitis. We show that before the genome is released, the Saffold virus 3 particle expands, and holes form in the previously compact capsid. These holes serve as channels for the release of the genome and small capsid proteins VP4 that in related enteroviruses facilitate subsequent transport of the virus genome into the cell cytoplasm.

Citovat

MULLAPUDI, Edukondalu; Jiří NOVÁČEK; Lenka PÁLKOVÁ; Pavel KULICH; A. Michael LINDBERG; Frank J. M. VAN KUPPEVELD a Pavel PLEVKA. Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč. 90, č. 17, s. 7628-7639. ISSN 0022-538X. Dostupné z: https://doi.org/10.1128/JVI.00746-16.

@article{1373938,
   author = {Mullapudi, Edukondalu and Nováček, Jiří and Pálková, Lenka and Kulich, Pavel and Lindberg, A. Michael and van Kuppeveld, Frank J. M. and Plevka, Pavel},
   article_location = {WASHINGTON},
   article_number = {17},
   doi = {https://doi.org/10.1128/JVI.00746-16},
   keywords = {HUMAN ENTEROVIRUS 71; COMMON COLD VIRUS; CRYOELECTRON MICROSCOPY; 3-DIMENSIONAL STRUCTURE; HUMAN RHINOVIRUS-2; CELLULAR RECEPTOR; THEILER VIRUS; POLIOVIRUS; PICORNAVIRUS; BINDING},
   language = {eng},
   issn = {0022-538X},
   journal = {JOURNAL OF VIROLOGY},
   title = {Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3},
   url = {http://jvi.asm.org/content/90/17/7628},
   volume = {90},
   year = {2016}
}

TY  - JOUR
ID  - 1373938
AU  - Mullapudi, Edukondalu - Nováček, Jiří - Pálková, Lenka - Kulich, Pavel - Lindberg, A. Michael - van Kuppeveld, Frank J. M. - Plevka, Pavel
PY  - 2016
TI  - Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3
JF  - JOURNAL OF VIROLOGY
VL  - 90
IS  - 17
SP  - 7628-7639
EP  - 7628-7639
PB  - AMER SOC MICROBIOLOGY
SN  - 0022538X
KW  - HUMAN ENTEROVIRUS 71
KW  - COMMON COLD VIRUS
KW  - CRYOELECTRON MICROSCOPY
KW  - 3-DIMENSIONAL STRUCTURE
KW  - HUMAN RHINOVIRUS-2
KW  - CELLULAR RECEPTOR
KW  - THEILER VIRUS
KW  - POLIOVIRUS
KW  - PICORNAVIRUS
KW  - BINDING
UR  - http://jvi.asm.org/content/90/17/7628
L2  - http://jvi.asm.org/content/90/17/7628
N2  - In order to initiate an infection, viruses need to deliver their genomes into cells. This involves uncoating the genome and transporting it to the cytoplasm. The process of genome delivery is not well understood for nonenveloped viruses. We address this gap in our current knowledge by studying the uncoating of the nonenveloped human cardiovirus Saffold virus 3 (SAFV-3) of the family Picornaviridae. SAFVs cause diseases ranging from gastrointestinal disorders to meningitis. We present a structure of a native SAFV-3 virion determined to 2.5 angstrom by X-ray crystallography and an 11-angstrom-resolution cryo-electron microscopy reconstruction of an "altered" particle that is primed for genome release. The altered particles are expanded relative to the native virus and contain pores in the capsid that might serve as channels for the release of VP4 subunits, N termini of VP1, and the RNA genome. Unlike in the related enteroviruses, pores in SAFV-3 are located roughly between the icosahedral 3- and 5-fold axes at an interface formed by two VP1 and one VP3 subunit. Furthermore, in native conditions many cardioviruses contain a disulfide bond formed by cysteines that are separated by just one residue. The disulfide bond is located in a surface loop of VP3. We determined the structure of the SAFV-3 virion in which the disulfide bonds are reduced. Disruption of the bond had minimal effect on the structure of the loop, but it increased the stability and decreased the infectivity of the virus. Therefore, compounds specifically disrupting or binding to the disulfide bond might limit SAFV infection. IMPORTANCE A capsid assembled from viral proteins protects the virus genome during transmission from one cell to another. However, when a virus enters a cell the virus genome has to be released from the capsid in order to initiate infection. This process is not well understood for nonenveloped viruses. We address this gap in our current knowledge by studying the genome release of Human Saffold virus 3. Saffold viruses cause diseases ranging from gastrointestinal disorders to meningitis. We show that before the genome is released, the Saffold virus 3 particle expands, and holes form in the previously compact capsid. These holes serve as channels for the release of the genome and small capsid proteins VP4 that in related enteroviruses facilitate subsequent transport of the virus genome into the cell cytoplasm.
ER  -

MULLAPUDI, Edukondalu; Jiří NOVÁČEK; Lenka PÁLKOVÁ; Pavel KULICH; A. Michael LINDBERG; Frank J. M. VAN KUPPEVELD a Pavel PLEVKA. Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3. \textit{JOURNAL OF VIROLOGY}. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč.~90, č.~17, s.~7628-7639. ISSN~0022-538X. Dostupné z: https://doi.org/10.1128/JVI.00746-16.

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