The Structure and Host Entry of an Invertebrate Parvovirus

MENG, Geng, Xinzheng ZHANG, Pavel PLEVKA, Qian YU, Peter TIJSSEN and Michael G. ROSSMANN. The Structure and Host Entry of an Invertebrate Parvovirus. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2013, vol. 87, No 23, p. 12523-12530. ISSN 0022-538X. Available from: https://dx.doi.org/10.1128/JVI.01822-13.

Basic information

• Original name: The Structure and Host Entry of an Invertebrate Parvovirus
• Authors: MENG, Geng, Xinzheng ZHANG, Pavel PLEVKA, Qian YU, Peter TIJSSEN and Michael G. ROSSMANN.
• Edition: JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2013, 0022-538X.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• Impact factor: Impact factor: 4.648
• Organization unit: Central European Institute of Technology
• Doi: http://dx.doi.org/10.1128/JVI.01822-13
• UT WoS: 000327183800002
• Tags: neMU

Abstract

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.