Molecular characteristics of Junin virus.
Results suggest that protein, glycerophospolipid, galactoside, and sialyl glycoside residues are present in Junin virus (JV), are accessible to enzymatic digestion, and play an important role in infection. Four major protein bands with molecular masses (Mr) 64 +/- 2, 56 +/- 2, 52 +/- 3 (mean +/- standard deviation, n = 4) and approximately 12-18 kDa were consistently detected after denaturing gel electrophoresis analysis of purified attenuated JV. The 52 kDa protein showed a diffuse tail in the 52-56 kDa range and was considered to be the JV glycoprotein. By Western blotting, the 64 kDa protein bound a JV neutralizing antibody and was considered to be the viral nucleoprotein. Additional bands corresponding to larger proteins (approximately 200, 96, 86, and 78 80 kDa in size), as well as fainter and broader bands in the 23-44 kDa region were also present in purified JV preparations. The relative resistance of virus infectivity to RNase digestion demonstrates that the genome of JV is protected from enzymatic attack. Analysis of purified JV virions by electrophoresis resolved the viral small (S) RNA and large (L) RNA species, 3636 +/- 54 bases and 7667 +/- 154 bases long, respectively (average length +/- range, in four determinations). The (S) RNA of attenuated JV appeared slightly larger than that reported for a pathogenic strain, ruling out a large sequence deletion as a reason for attenuation.
Bushar
G
G
Center for Devices and Radiological Health, Food and Drug Administration, Rockville, Maryland 20857, USA.
Sagripanti
J L
JL
D000818:Animals; D002522:Chlorocebus aethiops; D006801:Humans; D018051:Junin virus / Q000737:chemistry / Q000235:genetics* / Q000472:pathogenicity; D012367:RNA, Viral / Q000032:analysis; D014709:Vero Cells; D014764:Viral Proteins / Q000032:analysis / Q000235:genetics
D012367:RNA, Viral; D014764:Viral Proteins