PLEVKA, Pavel, Susan HAFENSTEIN, Katherine G. HARRIS, Javier O. CIFUENTE, Ying ZHANG, Valorie D. BOWMAN, Paul R. CHIPMAN, Carol M. BATOR, Feng LIN, M. Edward MEDOF and Michael G. ROSSMANN. Interaction of Decay-Accelerating Factor with Echovirus 7. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2010, vol. 84, No 24, p. 12665-12674. ISSN 0022-538X. Available from: https://dx.doi.org/10.1128/JVI.00837-10.
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Basic information
Original name Interaction of Decay-Accelerating Factor with Echovirus 7
Authors PLEVKA, Pavel, Susan HAFENSTEIN, Katherine G. HARRIS, Javier O. CIFUENTE, Ying ZHANG, Valorie D. BOWMAN, Paul R. CHIPMAN, Carol M. BATOR, Feng LIN, M. Edward MEDOF and Michael G. ROSSMANN.
Edition JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2010, 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: 5.189
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1128/JVI.00837-10
UT WoS 000284469600020
Keywords in English COMMON COLD VIRUS; DENSITY-LIPOPROTEIN RECEPTOR; CELLULAR RECEPTOR; HUMAN RHINOVIRUS-14; FACTOR CD55; FACTOR DAF; HUMAN ENTEROVIRUSES; COXSACKIEVIRUS B3; BINDING DOMAINS; PICORNAVIRUS
Tags neMU
Changed by Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 30/3/2017 11:06.
Abstract
Echovirus 7 (EV7) belongs to the Enterovirus genus within the family Picornaviridae. Many picornaviruses use IgG-like receptors that bind in the viral canyon and are required to initiate viral uncoating during infection. However, in addition, some of the enteroviruses use an alternative or additional receptor that binds outside the canyon. Decay-accelerating factor (DAF) has been identified as a cellular receptor for EV7. The crystal structure of EV7 has been determined to 3.1-angstrom resolution and used to interpret the 7.2-angstrom-resolution cryo-electron microscopy reconstruction of EV7 complexed with DAF. Each DAF binding site on EV7 is near a 2-fold icosahedral symmetry axis, which differs from the binding site of DAF on the surface of coxsackievirus B3, indicating that there are independent evolutionary processes by which DAF was selected as a picornavirus accessory receptor. This suggests that there is an advantage for these viruses to recognize DAF during the initial process of infection.
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