Partite expression of the bovine papillomavirus E1 open reading frame in Escherichia coli.
Six recombinants were constructed which expressed portions of the bovine papillomavirus E1 open reading frame as OmpF/E1/beta-galactosidase tribrid fusion proteins in Escherichia coli. Rabbit sera containing E1-specific antibodies were generated against five of these six fusion proteins (which together constitute 74% of the full-length E1 open reading frame). The individual fusion proteins and their cognate antisera will be useful reagents for defining the structure and function of the BPV E1 protein(s).
Wilson
V G
VG
Department of Medical Microbiology and Immunology, College of Medicine, Texas A & M University, College Station 77843.
Ludes-Meyers
J
J
D001425:Bacterial Outer Membrane Proteins / Q000235:genetics; D052688:Bovine papillomavirus 1 / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000096:biosynthesis* / Q000235:genetics* / Q000276:immunology; D004926:Escherichia coli / Q000235:genetics; D007106:Immune Sera / Q000096:biosynthesis; D016366:Open Reading Frames; D011233:Precipitin Tests; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D014764:Viral Proteins / Q000096:biosynthesis* / Q000235:genetics* / Q000276:immunology; D001616:beta-Galactosidase / Q000235:genetics
D001425:Bacterial Outer Membrane Proteins; D004268:DNA-Binding Proteins; C069814:E1 protein, Bovine papillomavirus; D007106:Immune Sera; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins; D001616:beta-Galactosidase