Virion Structure of Israeli Acute Bee Paralysis Virus

J 2016

Virion Structure of Israeli Acute Bee Paralysis Virus

MULLAPUDI, Edukondalu, Antonin PRIDAL, Lenka PÁLKOVÁ, Joachim R. DE MIRANDA, Pavel PLEVKA et. al.

Základní údaje

Originální název

Virion Structure of Israeli Acute Bee Paralysis Virus

Autoři

MULLAPUDI, Edukondalu (356 Indie, domácí), Antonin PRIDAL (203 Česká republika), Lenka PÁLKOVÁ (203 Česká republika, domácí), Joachim R. DE MIRANDA (752 Švédsko) a Pavel PLEVKA (203 Česká republika, garant, domácí)

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

Kód RIV

RIV/00216224:14740/16:00093719

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1128/JVI.00854-16

UT WoS

000382314100011

Klíčová slova anglicky

COLONY COLLAPSE DISORDER; 3-DIMENSIONAL STRUCTURE; POLIOVIRUS; RESOLUTION; PARTICLES; GENOME; LOSSES; CRYSTALLOGRAPHY; PICORNAVIRUSES; IDENTIFICATION

Štítky

rivok

Změněno: 27. 2. 2017 13:19, Mgr. Eva Špillingová

Anotace

V originále

The pollination services provided by the western honeybee (Apis mellifera) are critical for agricultural production and the diversity of wild flowering plants. However, honeybees suffer from environmental pollution, habitat loss, and pathogens, including viruses that can cause fatal diseases. Israeli acute bee paralysis virus (IAPV), from the family Dicistroviridae, has been shown to cause colony collapse disorder in the United States. Here, we present the IAPV virion structure determined to a resolution of 4.0 angstrom and and the structure of a pentamer of capsid protein protomers at a resolution of 2.7 angstrom. IAPV has major capsid proteins VP1 and VP3 with noncanonical jellyroll beta-barrel folds composed of only seven instead of eight beta-strands, as is the rule for proteins of other viruses with the same fold. The maturation of dicistroviruses is connected to the cleavage of precursor capsid protein VP0 into subunits VP3 and VP4. We show that a putative catalytic site formed by the residues Asp-Asp-Phe of VP1 is optimally positioned to perform the cleavage. Furthermore, unlike many picornaviruses, IAPV does not contain a hydrophobic pocket in capsid protein VP1 that could be targeted by capsid-binding antiviral compounds. IMPORTANCE Honeybee pollination is required for agricultural production and to sustain the biodiversity of wild flora. However, honeybee populations in Europe and North America are under pressure from pathogens, including viruses that cause colony losses. Viruses from the family Dicistroviridae can cause honeybee infections that are lethal, not only to individual honeybees, but to whole colonies. Here, we present the virion structure of an Aparavirus, Israeli acute bee paralysis virus (IAPV), a member of a complex of closely related viruses that are distributed worldwide. IAPV exhibits unique structural features not observed in other picorna-like viruses. Capsid protein VP1 of IAPV does not contain a hydrophobic pocket, implying that capsid-binding antiviral compounds that can prevent the replication of vertebrate picornaviruses may be ineffective against honeybee virus infections.

Citovat

MULLAPUDI, Edukondalu, Antonin PRIDAL, Lenka PÁLKOVÁ, Joachim R. DE MIRANDA a Pavel PLEVKA. Virion Structure of Israeli Acute Bee Paralysis Virus. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč. 90, č. 18, s. 8150-8159. ISSN 0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.00854-16.

@article{1373972,
   author = {Mullapudi, Edukondalu and Pridal, Antonin and Pálková, Lenka and de Miranda, Joachim R. and Plevka, Pavel},
   article_location = {WASHINGTON},
   article_number = {18},
   doi = {http://dx.doi.org/10.1128/JVI.00854-16},
   keywords = {COLONY COLLAPSE DISORDER; 3-DIMENSIONAL STRUCTURE; POLIOVIRUS; RESOLUTION; PARTICLES; GENOME; LOSSES; CRYSTALLOGRAPHY; PICORNAVIRUSES; IDENTIFICATION},
   language = {eng},
   issn = {0022-538X},
   journal = {JOURNAL OF VIROLOGY},
   title = {Virion Structure of Israeli Acute Bee Paralysis Virus},
   url = {http://jvi.asm.org/content/90/18/8150},
   volume = {90},
   year = {2016}
}

TY  - JOUR
ID  - 1373972
AU  - Mullapudi, Edukondalu - Pridal, Antonin - Pálková, Lenka - de Miranda, Joachim R. - Plevka, Pavel
PY  - 2016
TI  - Virion Structure of Israeli Acute Bee Paralysis Virus
JF  - JOURNAL OF VIROLOGY
VL  - 90
IS  - 18
SP  - 8150-8159
EP  - 8150-8159
PB  - AMER SOC MICROBIOLOGY
SN  - 0022538X
KW  - COLONY COLLAPSE DISORDER
KW  - 3-DIMENSIONAL STRUCTURE
KW  - POLIOVIRUS
KW  - RESOLUTION
KW  - PARTICLES
KW  - GENOME
KW  - LOSSES
KW  - CRYSTALLOGRAPHY
KW  - PICORNAVIRUSES
KW  - IDENTIFICATION
UR  - http://jvi.asm.org/content/90/18/8150
L2  - http://jvi.asm.org/content/90/18/8150
N2  - The pollination services provided by the western honeybee (Apis mellifera) are critical for agricultural production and the diversity of wild flowering plants. However, honeybees suffer from environmental pollution, habitat loss, and pathogens, including viruses that can cause fatal diseases. Israeli acute bee paralysis virus (IAPV), from the family Dicistroviridae, has been shown to cause colony collapse disorder in the United States. Here, we present the IAPV virion structure determined to a resolution of 4.0 angstrom and and the structure of a pentamer of capsid protein protomers at a resolution of 2.7 angstrom. IAPV has major capsid proteins VP1 and VP3 with noncanonical jellyroll beta-barrel folds composed of only seven instead of eight beta-strands, as is the rule for proteins of other viruses with the same fold. The maturation of dicistroviruses is connected to the cleavage of precursor capsid protein VP0 into subunits VP3 and VP4. We show that a putative catalytic site formed by the residues Asp-Asp-Phe of VP1 is optimally positioned to perform the cleavage. Furthermore, unlike many picornaviruses, IAPV does not contain a hydrophobic pocket in capsid protein VP1 that could be targeted by capsid-binding antiviral compounds. IMPORTANCE Honeybee pollination is required for agricultural production and to sustain the biodiversity of wild flora. However, honeybee populations in Europe and North America are under pressure from pathogens, including viruses that cause colony losses. Viruses from the family Dicistroviridae can cause honeybee infections that are lethal, not only to individual honeybees, but to whole colonies. Here, we present the virion structure of an Aparavirus, Israeli acute bee paralysis virus (IAPV), a member of a complex of closely related viruses that are distributed worldwide. IAPV exhibits unique structural features not observed in other picorna-like viruses. Capsid protein VP1 of IAPV does not contain a hydrophobic pocket, implying that capsid-binding antiviral compounds that can prevent the replication of vertebrate picornaviruses may be ineffective against honeybee virus infections.
ER  -

MULLAPUDI, Edukondalu, Antonin PRIDAL, Lenka PÁLKOVÁ, Joachim R. DE MIRANDA a Pavel PLEVKA. Virion Structure of Israeli Acute Bee Paralysis Virus. \textit{JOURNAL OF VIROLOGY}. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč.~90, č.~18, s.~8150-8159. ISSN~0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.00854-16.

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