The C domain in the surface envelope glycoprotein of subgroup C feline leukemia virus is a second receptor-binding domain
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منابع مشابه
Identification of Aptamer-Binding Sites in Hepatitis C Virus Envelope Glycoprotein E2
Hepatitis C Virus (HCV) encodes two envelope glycoproteins, E1 and E2. Our previous work selected a specific aptamer ZE2, which could bind to E2 with high affinity, with a great potential for developing new molecular probes as an early diagnostic reagents or therapeutic drugs targeting HCV. In this study, the binding sites between E2 and aptamer ZE2 were further explored. E2 was truncated to 15...
متن کاملHost range and receptor binding properties of vectors bearing feline leukemia virus subgroup B envelopes can be modulated by envelope sequences outside of the receptor binding domain.
To evaluate host range differences between two different strains of feline leukemia virus subgroup B (FeLV-B), we compared the binding and infectivity patterns of retrovirus vectors bearing either FeLV-B-90Z or FeLV-B-GA envelopes. We report here that the ability of these envelopes to utilize different Pit1 orthologs is mediated primarily by the receptor binding domain; however, in the case of ...
متن کاملA putative cell surface receptor for anemia-inducing feline leukemia virus subgroup C is a member of a transporter superfamily.
Domestic cats infected with the horizontally transmitted feline leukemia virus subgroup A (FeLV-A) often produce mutants (termed FeLV-C) that bind to a distinct cell surface receptor and cause severe aplastic anemia in vivo and erythroblast destruction in bone marrow cultures. The major determinant for FeLV-C-induced anemia has been mapped to a small region of the surface envelope glycoprotein ...
متن کاملComprehensive mapping of receptor-functioning domains in feline leukemia virus subgroup C receptor FLVCR1.
Infection of cells by the highly anemogenic feline leukemia virus subgroup C (FeLV-C) is mediated by the heme exporter FLVCR1, a cell surface protein containing 12 potential transmembrane segments with six presumptive extracellular loops (ECLs). To identify FLVCR1 residues critical for mediating FeLV-C infection, we first independently isolated a human cDNA encoding the FLVCR2 protein that shar...
متن کاملImmunogenic and Protective Potentials of Recombinant Receptor Binding Domain and a C-Terminal Fragment of Clostridium botulinum Neurotoxin Type E
Clostridium Botulinum Type E neurotoxin heavy chain consists of two domains: the translocation domain asthe N-terminal half and the binding domain as the Cterminal half (Hc). One effective way to neutralize botulinum neurotoxin is to inhibit binding of this toxin to neuromuscular synapses with antibodies against binding domain. Two synthetic genes, coding for Hc (the full length binding d...
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ژورنال
عنوان ژورنال: Virology
سال: 2008
ISSN: 0042-6822
DOI: 10.1016/j.virol.2007.09.011