Počet záznamů: 1
Nonconserved tryptophan 38 of the cell surface receptor for subgroup J avian leukosis virus discriminates sensitive from resistant avian species
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SYSNO ASEP 0395911 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Nonconserved tryptophan 38 of the cell surface receptor for subgroup J avian leukosis virus discriminates sensitive from resistant avian species Tvůrce(i) Kučerová, Dana (UMG-J)
Plachý, Jiří (UMG-J) RID
Reinišová, Markéta (UMG-J)
Šenigl, Filip (UMG-J) RID
Trejbalová, Kateřina (UMG-J) RID
Geryk, Josef (UMG-J) RID
Hejnar, Jiří (UMG-J) RIDZdroj.dok. Journal of Virology - ISSN 0022-538X
Roč. 87, č. 15 (2013), s. 8399-8407Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova avian leukosis virus ; ALV-J ; NHE1 ; host resistance ; receptor Vědní obor RIV EB - Genetika a molekulární biologie CEP GAP502/10/1651 GA ČR - Grantová agentura ČR Institucionální podpora UMG-J - RVO:68378050 UT WOS 000321590200013 DOI 10.1128/JVI.03180-12 Anotace Subgroup J avian leukosis virus (ALV-J) is unique among the avian sarcoma and leukosis viruses in using the multimembrane-spanning cell surface protein Na+/H+ exchanger type 1 (NHE1) as a receptor. The precise localization of amino acids critical for NHE1 receptor activity is key in understanding the virus-receptor interaction and potential interference with virus entry. Because no resistant chicken lines have been described until now, we compared the NHE1 amino acid sequences from permissive and resistant galliform species. In all resistant species, the deletion or substitution of W38 within the first extracellular loop was observed either alone or in the presence of other incidental amino acid changes. Using the ectopic expression of wild-type or mutated chicken NHE1 in resistant cells and infection with a reporter recombinant retrovirus of subgroup J specificity, we studied the effect of individual mutations on the NHE1 receptor capacity. We suggest that the absence of W38 abrogates binding of the subgroup J envelope glycoprotein to ALV-J- resistant cells. Altogether, we describe the functional importance of W38 for virus entry and conclude that natural polymorphisms in NHE1 can be a source of host resistance to ALV-J. Pracoviště Ústav molekulární genetiky Kontakt Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Rok sběru 2014
Počet záznamů: 1