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Volume 271, Number 40,
Issue of October 4, 1996
pp. 24728-24735
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Specific Interaction in Vitro and in Vivo
of Glyceraldehyde-3-phosphate Dehydrogenase and LA Protein with
Cis-acting RNAs of Human Parainfluenza Virus Type 3
(Received for publication, March 27, 1996, and in revised form, July 15, 1996)
Bishnu P.
De
,
Sanhita
Gupta
,
Hong
Zhao
,
Judith A.
Drazba
§
and
Amiya K.
Banerjee
From the Departments of Molecular Biology and
§ Neurosciences, Research Institute, The Cleveland Clinic
Foundation, Cleveland, Ohio 44195
Human parainfluenza virus type 3 (HPIV3) genome
RNA is transcribed and replicated by the virus-encoded
RNA-dependent RNA polymerase, and specific cellular
proteins play a regulatory role in these processes. To search for
cellular proteins potentially interacting with HPIV3 cis-acting
regulatory RNAs, a gel mobility shift assay was used. Two cellular
proteins specifically interacted with the viral cis-acting RNAs
containing the genomic 3 -noncoding region and the plus-sense leader
sequence region. Surprisingly, by biochemical and immunological
analyses, one of the cellular proteins was identified as the key
glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH).
The other protein was characterized as the autoantigen, LA protein.
Both GAPDH and LA protein also interacted with the same cis-acting RNA
sequences in vivo and were found to be associated with the
HPIV3 ribonucleoprotein complex in the infected cells. By double
immunofluorescent labeling, GAPDH was found to be co-localized with
viral ribonucleoprotein in the perinuclear region. These observations
strongly suggest that cellular GAPDH and LA Protein participate in the
regulation of HPIV3 gene expression.

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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.
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