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 a Michael G. ROSSMANN. Interaction of Decay-Accelerating Factor with Echovirus 7. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2010, roč. 84, č. 24, s. 12665-12674. ISSN 0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.00837-10.
Další formáty:   BibTeX LaTeX RIS
Základní údaje
Originální název Interaction of Decay-Accelerating Factor with Echovirus 7
Autoři 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 a Michael G. ROSSMANN.
Vydání JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2010, 0022-538X.
Další údaje
Originální 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: 5.189
Organizační jednotka Středoevropský technologický institut
Doi http://dx.doi.org/10.1128/JVI.00837-10
UT WoS 000284469600020
Klíčová slova anglicky COMMON COLD VIRUS; DENSITY-LIPOPROTEIN RECEPTOR; CELLULAR RECEPTOR; HUMAN RHINOVIRUS-14; FACTOR CD55; FACTOR DAF; HUMAN ENTEROVIRUSES; COXSACKIEVIRUS B3; BINDING DOMAINS; PICORNAVIRUS
Štítky neMU
Změnil Změnila: Mgr. Eva Špillingová, učo 110713. Změněno: 30. 3. 2017 11:06.
Anotace
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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