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Článek

FT
PubMed

Záznam pochází z PubMed

Two different molecular defects in the Tva receptor gene explain the resistance of two tvar lines of chickens to infection by subgroup A avian sarcoma and leukosis viruses

Journal of virology. 2004 Dec ; 78 (24) : 13489-500.

J Virol
ISSN 0022-538X
Zdroj

Jazyk angličtina Země Spojené státy americké Médium print

Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, P.H.S.

Perzistentní odkaz https://www.medvik.cz/link/pmid15564460

Grantová podpora
R01 AI048682 NIAID NIH HHS - United States
AI48682 NIAID NIH HHS - United States

Online Plný text

PubMed 15564460
PubMed Central PMC533904
DOI 10.1128/jvi.78.24.13489-13500.2004
PII: 78/24/13489
Knihovny.cz E-zdroje

MeSH
křepelky a křepelovití MeSH
kultivované buňky MeSH
kur domácí imunologie virologie MeSH
kuřecí embryo MeSH
molekulární sekvence - údaje MeSH
mutace * MeSH
ptačí leukóza imunologie virologie MeSH
ptačí proteiny MeSH
ptačí sarkom imunologie virologie MeSH
sekvence aminokyselin MeSH
sekvence nukleotidů MeSH
sekvenční analýza DNA MeSH
virové receptory chemie genetika metabolismus MeSH
virus ptačí leukózy metabolismus patogenita MeSH
viry ptačího sarkomu metabolismus patogenita MeSH
zvířata MeSH
Check Tag
kuřecí embryo MeSH
zvířata MeSH
Publikační typ
časopisecké články MeSH
práce podpořená grantem MeSH
Research Support, U.S. Gov't, P.H.S. MeSH
Názvy látek
ptačí proteiny MeSH
Tva receptor MeSH Prohlížeč
virové receptory MeSH

The subgroup A to E avian sarcoma and leukosis viruses (ASLVs) are highly related and are thought to have evolved from a common ancestor. These viruses use distinct cell surface proteins as receptors to gain entry into avian cells. Chickens have evolved resistance to infection by the ASLVs. We have identified the mutations responsible for the block to virus entry in chicken lines resistant to infection by subgroup A ASLVs [ASLV(A)]. The tva genetic locus determines the susceptibility of chicken cells to ASLV(A) viruses. In quail, the ASLV(A) susceptibility allele tva(s) encodes two forms of the Tva receptor; these proteins are translated from alternatively spliced mRNAs. The normal cellular function of the Tva receptor is unknown; however, the extracellular domain contains a 40-amino-acid, cysteine-rich region that is homologous to the ligand binding region of the low-density lipoprotein receptor (LDLR) proteins. The chicken tva(s) cDNAs had not yet been fully characterized; we cloned the chicken tva cDNAs from two lines of subgroup A-susceptible chickens, line H6 and line 0. Two types of chicken tva(s) cDNAs were obtained. These cDNAs encode a longer and shorter form of the Tva receptor homologous to the Tva forms in quail. Two different defects were identified in cDNAs cloned from two different ASLV(A)-resistant inbred chickens, line C and line 7(2). Line C tva(r) contains a single base pair substitution, resulting in a cysteine-to-tryptophan change in the LDLR-like region of Tva. This mutation drastically reduces the binding affinity of Tva(R) for the ASLV(A) envelope glycoproteins. Line 7(2) tva(r2) contains a 4-bp insertion in exon 1 that causes a change in the reading frame, which blocks expression of the Tva receptor.

Department of Cellular and Viral Genetics Institute of Molecular Genetics Academy of Sciences of the Czech Republic Prague

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