2013
The Structure and Host Entry of an Invertebrate Parvovirus
MENG, Geng, Xinzheng ZHANG, Pavel PLEVKA, Qian YU, Peter TIJSSEN et. al.Základní údaje
Originální název
The Structure and Host Entry of an Invertebrate Parvovirus
Autoři
MENG, Geng, Xinzheng ZHANG, Pavel PLEVKA, Qian YU, Peter TIJSSEN a Michael G. ROSSMANN
Vydání
JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2013, 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: 4.648
Organizační jednotka
Středoevropský technologický institut
UT WoS
000327183800002
Štítky
Změněno: 29. 3. 2017 11:08, Mgr. Eva Špillingová
Anotace
V originále
The 3.5-angstrom resolution X-ray crystal structure of mature cricket parvovirus (Acheta domesticus densovirus [AdDNV]) has been determined. Structural comparisons show that vertebrate and invertebrate parvoviruses have evolved independently, although there are common structural features among all parvovirus capsid proteins. It was shown that raising the temperature of the AdDNV particles caused a loss of their genomes. The structure of these emptied particles was determined by cryo-electron microscopy to 5.5-angstrom resolution, and the capsid structure was found to be the same as that for the full, mature virus except for the absence of the three ordered nucleotides observed in the crystal structure. The viral protein 1 (VP1) amino termini could be externalized without significant damage to the capsid. In vitro, this externalization of the VP1 amino termini is accompanied by the release of the viral genome.