Dongwan Yoo
Professor, Pathobiology
Professional Interests: We are
working on arteriviruses. These viruses belong to a unique group of animal
viruses, called the family Arterividae in the order Nidovirales .
The term "nidovirus" comes from the process of a nested set
of mRNA transcribed during virus replication. Nidoviruses are grouped
into the Coronaviridae family and the Arteriviridae family.
SARS virus belongs to Coronaviridae and PRRS (porcine reproductive
and respiratory syndrome) virus that we are currently working belongs
to Arteriviridae .
Porcine reproductive and respiratory syndrome virus (PRRSV)
PRRSV is an emerged virus in pigs. This virus emerged
a decade ago in North America and Europe independently, and is now found
worldwide. PRRSV infection results in acute reproductive failure in pregnant
sows and severe respiratory illness in young pigs. PRRSV genome is a
single-stranded, non-segmented, positive-sense RNA of approximately 15
Kb in size.
1) Full-length infectious cDNA clone and "reverse
genetics" (see
a paper related to this research)
In the positive-strand RNA virus
system, infectious cDNA clones are the most powerful tool to study viruses
at the molecular level. We have completed cloning and sequencing of the
full-length genomic RNA of PRRSV, and full-length infectious cDNA clones
have been made. The full-length clone is infectious in cultured cell and
infectious progeny is generated when transfected. Using infectious clones,
numerous PRRSV mutants have been constructed to contain specific modifications
on the viral genome, and these recombinant viruses are studied for their
genotypes and phenotypes. This system is referred to "reverse genetics".
We are interested in the pathogenic role that individual viral proteins
play during infection and their interaction with cellular proteins.
2) Nuclear function of the viral capsid protein (see
a paper related to this research)
PRRSV replication takes place in the cytoplasm, and
thus the nuclear function of the cell is not required for PRRSV replication.
The capsid protein of PRRSV however is specifically localized in the
nucleus of virus-infected cell, and we are interested in the biological
function of the capsid protein in the nucleus. Using the yeast two-hybrid
system, we have identified several cellular proteins interacting with
the PRRSV capsid protein, and these proteins appear to be involved in
the various pathways of cellular signal transduction. We are presently
expanding our research to capsid proteins of other arteriviruses including
equine arteritis virus (EAV), lactate dehydrogenase elevating virus (LDV),
and simian hemorrhagic fever virus (SHFV).
Selected Publications:
Lee C, and Yoo D (2006) The small envelope protein of PRRSV possesses ion channel protein-like properties. Virology 355:30-43.
Lee C, Hodgins DC , Calvert JG, Welch SK , Jolie R, and Yoo D (2006) Mutations in the nuclear localization signal of the PRRSV nucleocapsid protein attenuate virus replication. Virology 346: 238-250 (Cover page article in volume 346, issue 1).
Lee C, and Yoo D (2005) Cysteine residues of the PRRSV small envelope protein are non-essential for virus infectivity. J Gen Virol. 86:3091-3096.
Lee C, Welch SK, Calvert JG, and Yoo D (2005) A DNA-launched reverse genetics system for PRRSV reveals that homodimerization of the nucleocapsid protein is essential for virus infectivity. Virology 331:47-62.
Yoo D, Wootton S, Li G, Song C, and Rowland RR (2003) Colocalization and interaction of the PRRSV nucleocapsid protein with the small nucleolar RNA-associated protein fibrillarin. J Virol. 77:12173-12183.
Rowland RR, Schneider P, Fang Y, Wootton S, Yoo D, and Benfield DA (2003) Peptide domains involved in the localization of the PRRSV nuclocapsid protein to the nucleolus. Virology 316:135-145.
Kovacs-Nolan J, Yoo D, and Mine Y (2003). Fine mapping of the neutralizing epitopes on the VP8 subunit protein of human rotavirus. Biochemical J. 376:269-275.
Wu HY, Guy JC, Yoo D, Vlasak R, Urbach E, and Brian DA (2003). Common RNA replication signals exist among group 2 coronaviruses despite a two cluster pattern of 5' and 3' UTR sequences. Virology 315:174-183.
Rowland RR, and Yoo D (2003). Nucleolar-cytoplasmic shuttling of PRRSV nucleocapsid protein: a simple case of molecular mimicry or the complex regulation by nuclear import, nucleolar localization and nuclear export signal sequences (Invited Review). Virus Res. 95:23-33.
Wootton S, and Yoo D (2003) Homo-oligomerization of the PRRSV nucleocapsid protein and the role of disulfide linkages. J Virol. 77:4546-4557.
Wootton S, Rowland RR, and Yoo D (2002) Phosphorylation of the nucleocapsid protein of PRRSV. J Virol. 76:10569-10576.
