title: Isolation of equine infectious anemia virus glycoproteins. Lectin affinity chromatography procedures for high avidity glycoproteins.
abstract: Lectin affinity chromatography procedures were evaluated for the isolation of enveloped virus glycoproteins. The major glycoprotein of equine infectious anemia virus (EIAV) bound to concanavalin A (Con A)-Sepharose through interactions which could not be reversed by alpha-methylglucoside, but elution could be accomplished with buffers containing guanidine hydrochloride or sodium dodecyl sulfate. These denaturants, however, also released about one-half of the Con A protein from the Sepharose matrix. This degradation does not appear to have been recognized previously, as denaturants are frequently employed for the isolation of virus glycoproteins from Con A-Sepharose. In contrast, the virus glycoprotein bound equally well to Sepharose-bound Lens culinaris (lentil) lectin affinity columns and was effectively eluted with buffer containing 0.2 M alpha-methylglucoside. The lentil lectin-Sepharose procedure described is rapid, inexpensive and results in the efficient separation and recovery of EIAV glycoproteins. Thus, lentil lectin-Sepharose can provide a useful alternative to Con A-Sepharose for isolating other high avidity glycoproteins from viral envelopes or cell membranes.
mesh_terms: D002846:Chromatography, Affinity / Q000379:methods; D003208:Concanavalin A; D006023:Glycoproteins / Q000302:isolation & purification*; D004860:Infectious Anemia Virus, Equine / Q000032:analysis*; D037102:Lectins; D011489:Protein Denaturation; D012997:Solvents; D014764:Viral Proteins / Q000302:isolation & purification*
chemical_list: D006023:Glycoproteins; D037102:Lectins; D012997:Solvents; D014764:Viral Proteins; D003208:Concanavalin A