Lectin affinity of Junin virus glycoproteins.
We studied the binding of Junin virus (Arenaviridae) glycoproteins, G1 and G2, to two insolubilized lectins. The results showed that mannose, N-acetyl-glucosamine and galactose residues were exposed on G2, while only the latter predominated on G1. Heterogeneity of carbohydrate chains was found in G2, the only glycoprotein that was iodinated by the lactoperoxidase method.
Mersich
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SE
Cátedra de Virología, Facultad de Cs Exactas y Naturales, UBA, Ciudad Universitaria, Buenos Aires.
Castilla
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V
Damonte
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EB
D000818:Animals; D001116:Arenaviridae / Q000378:metabolism*; D006477:Arenaviruses, New World / Q000378:metabolism*; D002846:Chromatography, Affinity; D007784:Lactoperoxidase / Q000378:metabolism; D037102:Lectins / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism*; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000378:metabolism*
D037102:Lectins; D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins; D007784:Lactoperoxidase