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Characterization of a Conformationally Sensitive Epitope on Moloney Murine Leukemia Virus gp70

Characterization of a Conformationally Sensitive Epitope on Moloney Murine Leukemia Virus gp70 We describe here several properties of a conformationally sensitive epitope common to the Moloney (M) and Rauscher (R) murine leukemia virus (MLV) gp70 family of glycoproteins, e.g., M-MLV gp70 and R-MLV gp71. This epitope was not detected by western blotting or by enzyme-linked immunosorbent assay experiments with three different lots of polyclonal R-MLV gp69/71 sera. However, it was detected when a specific monoclonal antibody, R47, was used in western blotting or immuno-dot-blotting experiments with the two viruses. R47 maps to a central 14-kd segment on R-MLV gp71 which spans an important structural domain, namely, that corresponding to the recombination site between ecotropic and endogenous envelope glycoprotein-coding sequences. Analysis of the western as well as dot blots developed with the R47 monoclonal antibody showed that about a 25-fold higher affinity for the epitope existed on R-MLV gp71, relative to M-MLV gp70. It thus appears that R-MLV and M-MLV gp70, although very closely related both structurally and serologically, are conformationally distinct in one domain, namely, the site of recombination between ecotropic and endogenous gp70-coding sequences. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Intervirology Karger

Characterization of a Conformationally Sensitive Epitope on Moloney Murine Leukemia Virus gp70

Trauger, Richard; Rayfield, Mark A.; Luftig, Ronald B.
Intervirology , Volume 28 (1): 10 – Jan 1, 2008
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Publisher
Karger
Copyright
© 1987 S. Karger AG, Basel
ISSN
0300-5526
eISSN
1423-0100
DOI
10.1159/000149995
Publisher site
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Abstract

We describe here several properties of a conformationally sensitive epitope common to the Moloney (M) and Rauscher (R) murine leukemia virus (MLV) gp70 family of glycoproteins, e.g., M-MLV gp70 and R-MLV gp71. This epitope was not detected by western blotting or by enzyme-linked immunosorbent assay experiments with three different lots of polyclonal R-MLV gp69/71 sera. However, it was detected when a specific monoclonal antibody, R47, was used in western blotting or immuno-dot-blotting experiments with the two viruses. R47 maps to a central 14-kd segment on R-MLV gp71 which spans an important structural domain, namely, that corresponding to the recombination site between ecotropic and endogenous envelope glycoprotein-coding sequences. Analysis of the western as well as dot blots developed with the R47 monoclonal antibody showed that about a 25-fold higher affinity for the epitope existed on R-MLV gp71, relative to M-MLV gp70. It thus appears that R-MLV and M-MLV gp70, although very closely related both structurally and serologically, are conformationally distinct in one domain, namely, the site of recombination between ecotropic and endogenous gp70-coding sequences.

Journal

Intervirology – Karger

Published: Jan 1, 2008

Keywords: Western blotting; Moloney murine leukemia virus; Envelope glycoprotein; Monoclonal antibody; gp70 epitope

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