Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen

J 2011

Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen

KAUFMANN, Baerbel, Mohamed EL-FAR, Pavel PLEVKA, Valorie D. BOWMAN, Yi LI et. al.

Základní údaje

Originální název

Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen

Autoři

KAUFMANN, Baerbel, Mohamed EL-FAR, Pavel PLEVKA, Valorie D. BOWMAN, Yi LI, Peter TIJSSEN a Michael G. ROSSMANN

Vydání

JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2011, 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

Impakt faktor

Impact factor: 5.402

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1128/JVI.02688-10

UT WoS

000289787300006

Klíčová slova anglicky

CAPSID PROTEIN; ANGSTROM RESOLUTION; CANINE PARVOVIRUS; MINUTE VIRUS; NMR SYSTEM; CRYSTALLOGRAPHY; INFECTIVITY; ENZYME; MICE; A(2)

Štítky

neMU

Změněno: 29. 3. 2017 15:02, Mgr. Eva Špillingová

Anotace

V originále

Bombyx mori densovirus 1 (BmDNV-1), a major pathogen of silkworms, causes significant losses to the silk industry. The structure of the recombinant BmDNV-1 virus-like particle has been determined at 3.1-angstrom resolution using X-ray crystallography. It is the first near-atomic-resolution structure of a virus-like particle within the genus Iteravirus. The particles consist of 60 copies of the 55-kDa VP3 coat protein. The capsid protein has a beta-barrel "jelly roll" fold similar to that found in many diverse icosahedral viruses, including archaeal, bacterial, plant, and animal viruses, as well as other parvoviruses. Most of the surface loops have little structural resemblance to other known parvovirus capsid proteins. In contrast to vertebrate parvoviruses, the N-terminal beta-strand of BmDNV-1 VP3 is positioned relative to the neighboring 2-fold related subunit in a "domain-swapped" conformation, similar to findings for other invertebrate parvoviruses, suggesting domain swapping is an evolutionarily conserved structural feature of the Densovirinae.

Citovat

KAUFMANN, Baerbel, Mohamed EL-FAR, Pavel PLEVKA, Valorie D. BOWMAN, Yi LI, Peter TIJSSEN a Michael G. ROSSMANN. Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2011, roč. 85, č. 10, s. 4691-4697. ISSN 0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.02688-10.

@article{1376822,
   author = {Kaufmann, Baerbel and ElandFar, Mohamed and Plevka, Pavel and Bowman, Valorie D. and Li, Yi and Tijssen, Peter and Rossmann, Michael G.},
   article_location = {WASHINGTON},
   article_number = {10},
   doi = {http://dx.doi.org/10.1128/JVI.02688-10},
   keywords = {CAPSID PROTEIN; ANGSTROM RESOLUTION; CANINE PARVOVIRUS; MINUTE VIRUS; NMR SYSTEM; CRYSTALLOGRAPHY; INFECTIVITY; ENZYME; MICE; A(2)},
   language = {eng},
   issn = {0022-538X},
   journal = {JOURNAL OF VIROLOGY},
   title = {Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen},
   volume = {85},
   year = {2011}
}

TY  - JOUR
ID  - 1376822
AU  - Kaufmann, Baerbel - El-Far, Mohamed - Plevka, Pavel - Bowman, Valorie D. - Li, Yi - Tijssen, Peter - Rossmann, Michael G.
PY  - 2011
TI  - Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen
JF  - JOURNAL OF VIROLOGY
VL  - 85
IS  - 10
SP  - 4691-4697
EP  - 4691-4697
PB  - AMER SOC MICROBIOLOGY
SN  - 0022538X
KW  - CAPSID PROTEIN
KW  - ANGSTROM RESOLUTION
KW  - CANINE PARVOVIRUS
KW  - MINUTE VIRUS
KW  - NMR SYSTEM
KW  - CRYSTALLOGRAPHY
KW  - INFECTIVITY
KW  - ENZYME
KW  - MICE
KW  - A(2)
N2  - Bombyx mori densovirus 1 (BmDNV-1), a major pathogen of silkworms, causes significant losses to the silk industry. The structure of the recombinant BmDNV-1 virus-like particle has been determined at 3.1-angstrom resolution using X-ray crystallography. It is the first near-atomic-resolution structure of a virus-like particle within the genus Iteravirus. The particles consist of 60 copies of the 55-kDa VP3 coat protein. The capsid protein has a beta-barrel "jelly roll" fold similar to that found in many diverse icosahedral viruses, including archaeal, bacterial, plant, and animal viruses, as well as other parvoviruses. Most of the surface loops have little structural resemblance to other known parvovirus capsid proteins. In contrast to vertebrate parvoviruses, the N-terminal beta-strand of BmDNV-1 VP3 is positioned relative to the neighboring 2-fold related subunit in a "domain-swapped" conformation, similar to findings for other invertebrate parvoviruses, suggesting domain swapping is an evolutionarily conserved structural feature of the Densovirinae.
ER  -

KAUFMANN, Baerbel, Mohamed EL-FAR, Pavel PLEVKA, Valorie D. BOWMAN, Yi LI, Peter TIJSSEN a Michael G. ROSSMANN. Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen. \textit{JOURNAL OF VIROLOGY}. WASHINGTON: AMER SOC MICROBIOLOGY, 2011, roč.~85, č.~10, s.~4691-4697. ISSN~0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.02688-10.

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