TY - JOUR
T1 - Two antiviral proteins from tobacco
T2 - Purification and characterization by monoclonal antibodies to human β-interferon
AU - Edelbaum, Orit
AU - Ilan, Neta
AU - Grafi, Gideon
AU - Sher, Naamit
AU - Stram, Yehuda
AU - Novick, Daniela
AU - Tal, Natan
AU - Sela, Ilan
AU - Rubinstein, Menachem
PY - 1990
Y1 - 1990
N2 - Polyclonal antibodies to human β-interferon reacted specifically with two plant proteins (gp22 and gp35) by Western blot analysis of crude protein extracts from tobacco leaves infected with tobacco mosaic virus. Immunoaffinity chromatographv of these extracts on a column of immobilized monoclonal antibodies to human β-interferon and then reversed-phase HPLC yielded gp22 and gp35 in a pure state. Both proteins reacted with the Schiff reagent and concanavalin A (indicating their glycoprotein nature) and exhibited antiviral activity (inhibiting tobacco mosaic virus replication in tobaccoleaf discs at concentrations of ng/ml). Each protein was cleaved by cyanogen bromide and the resultant peptides, separated by HPLC, were sequenced as far as the Edman degradation allowed, giving a total of 61 amino acid residues for gp22 and 105 residues for gp35, which represent 30-50% of their expected length. Computer analyses of the sequenced segments revealed no significant homology to human β-interferon, each other, or any other recorded sequence.
AB - Polyclonal antibodies to human β-interferon reacted specifically with two plant proteins (gp22 and gp35) by Western blot analysis of crude protein extracts from tobacco leaves infected with tobacco mosaic virus. Immunoaffinity chromatographv of these extracts on a column of immobilized monoclonal antibodies to human β-interferon and then reversed-phase HPLC yielded gp22 and gp35 in a pure state. Both proteins reacted with the Schiff reagent and concanavalin A (indicating their glycoprotein nature) and exhibited antiviral activity (inhibiting tobacco mosaic virus replication in tobaccoleaf discs at concentrations of ng/ml). Each protein was cleaved by cyanogen bromide and the resultant peptides, separated by HPLC, were sequenced as far as the Edman degradation allowed, giving a total of 61 amino acid residues for gp22 and 105 residues for gp35, which represent 30-50% of their expected length. Computer analyses of the sequenced segments revealed no significant homology to human β-interferon, each other, or any other recorded sequence.
UR - http://www.scopus.com/inward/record.url?scp=0025166444&partnerID=8YFLogxK
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C2 - 2300549
AN - SCOPUS:0025166444
SN - 0027-8424
VL - 87
SP - 588
EP - 592
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 2
ER -