Replacement of the V3 domain in the surface subunit of the feline immunodeficiency virus envelope glycoprotein with the equivalent region of a T cell-tropic human immunodeficiency virus type 1 results in a chimeric surface protein that efficiently binds to CXCR4

Feline immunodeficiency virus (FIV) and the T cell-tropic strains of human immunodeficiency virus type 1 (HIV-1) share the use of the chemokine receptor CXCR4 for cell entry. To study this process further we developed a cell surface binding assay based on the expression of a soluble version of the F...

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Detalles Bibliográficos
Autores principales: González, S.A., Falcón, J.I., Affranchino, J.L.
Formato: JOUR
Materias:
binding protein
chemokine receptor CXCR4
chimeric protein
glycoprotein E1
Influenza virus hemagglutinin
membrane protein
monoclonal antibody
plerixafor
virus envelope protein
article
binding assay
cell fusion
cell surface
controlled study
electrophoretic mobility
embryo
enzyme linked immunosorbent assay
Feline immunodeficiency virus
flow cytometry
human
human cell
Human immunodeficiency virus 1
immunoblotting
polyacrylamide gel electrophoresis
priority journal
protein expression
protein subunit
quantitative analysis
quantitative assay
site directed mutagenesis
surface property
T lymphocyte
target cell
virus entry
Western blotting
Animals
Cell Line
env Gene Products, Human Immunodeficiency Virus
Glycoproteins
HIV-1
Humans
Immunodeficiency Virus, Feline
Receptors, CXCR4
Receptors, HIV
Recombination, Genetic
Viral Envelope Proteins
Virus Attachment
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_08892229_v30_n3_p250_Gonzalez
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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