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Journal of Virology, September 1999, p. 7761-7768, Vol. 73, No. 9
James A. Baker Institute, College of
Veterinary Medicine, Cornell University, Ithaca, New York 14853
Received 16 March 1999/Accepted 28 May 1999
Phage display of cDNA clones prepared from feline cells was used to
identify host cell proteins that bound to DNA-containing feline
panleukopenia virus (FPV) capsids but not to empty capsids. One gene
found in several clones encoded a heterogeneous nuclear ribonucleoprotein (hnRNP)-related protein (DBP40) that was very similar
in sequence to the A/B-type hnRNP proteins. DBP40 bound specifically to
oligonucleotides representing a sequence near the 5' end of the genome
which is exposed on the outside of the full capsid but did not bind
most other terminal sequences. Adding purified DBP40 to an in vitro
fill-in reaction using viral DNA as a template inhibited the production
of the second strand after nucleotide (nt) 289 but prior to nt 469. DBP40 bound to various regions of the viral genome, including a region
between nt 295 and 330 of the viral genome which has been associated
with transcriptional attenuation of the parvovirus minute virus of
mice, which is mediated by a stem-loop structure of the DNA and
cellular proteins. Overexpression of the protein in feline cells from a
plasmid vector made them largely resistant to FPV infection.
Mutagenesis of the protein binding site within the 5' end viral genome
did not affect replication of the virus.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
A Heterogeneous Nuclear Ribonucleoprotein A/B-Related Protein
Binds to Single-Stranded DNA near the 5' End or within the Genome of
Feline Parvovirus and Can Modify Virus Replication
*
Corresponding author. Mailing address: James A. Baker
Institute, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853. Phone: (607) 256-5649. Fax: (607) 256-5608. E-mail: crp3{at}cornell.edu.
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