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.

Basic information

Original name

Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen

Authors

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

Edition

JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2011, 0022-538X

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 5.402

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000289787300006

Keywords in English

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

Abstract

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 and Michael G. ROSSMANN. Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2011, vol. 85, No 10, p. 4691-4697. ISSN 0022-538X. Available from: 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 and Michael G. ROSSMANN. Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen. \textit{JOURNAL OF VIROLOGY}. WASHINGTON: AMER SOC MICROBIOLOGY, 2011, vol.~85, No~10, p.~4691-4697. ISSN~0022-538X. Available from: https://dx.doi.org/10.1128/JVI.02688-10.

Detailed Information on Publication Record