About

Dr. Dongwan Yoo is a Professor of Virology in the Department of Pathobiology at the College of Veterinary Medicine, University of Illinois Urbana-Champaign. His research focuses on the molecular and cellular aspects of viral infections, particularly arteriviruses and coronaviruses, with the aim of developing control measures against infections of medical and veterinary importance. He investigates how innate immunity reacts to invading viruses and how viruses evade host immune surveillance to ensure their survival and replication. Dr. Yoo employs a reverse genetics system to engineer viral RNA genomes and generate mutant viruses to study pathogenic mechanisms in cells and animals. He studied veterinary medicine at Seoul National University in Korea, where he also completed his MSc in microbiology. He further advanced his virology expertise at the University of Ottawa in Canada, completing a PhD. His professional experience includes positions as Assistant Professor and Associate Professor at the Ontario Veterinary College, University of Guelph, and a Special Appointment at Seoul National University. He has also served as a Visiting Professor at Leiden University Medical Center in the Netherlands. Dr. Yoo moved to the University of Illinois to pursue his research endeavors, contributing significantly to the understanding of viral immune modulation, evasion strategies, and vaccine development, with numerous publications and ongoing projects in these areas.

Research topics

• Biology
• Virology
• Immunology
• Medicine
• Pathology
• Genetics

Selected publications

• An alternative reverse genetics system for PRRS virus and its application to define the role of endocytic sorting signal in GP3 protein intracellular trafficking

  Frontiers in Microbiology · 2026-03-10 · 1 citations

  articleOpen accessSenior author

  Porcine reproductive and respiratory syndrome virus (PRRSV) glycoprotein 3 (GP3) forms a heterotrimeric complex with GP2 and GP4, which is essential for viral entry and assembly. However, the intracellular trafficking mechanisms governing GP3 localization and incorporation into virions remain incompletely understood. Here, we identified two highly conserved tyrosine-based sorting signals (YxxΦ) within GP3, motifs that mediate adaptor protein–dependent trafficking through the secretory and endocytic pathways. To define the functional roles of these motifs, we established a Linear Overlapping Infectious Polymerase Amplicon (LOIPA)–based reverse-genetics system for PRRSV. This system enabled precise reconstitution of full-length viral genomes from overlapping cDNA fragments and facilitated rapid introduction of site-specific mutations without bacterial cloning. Using LOIPA, we generated a set of recombinant PRRSV mutants carrying targeted substitutions within the two GP3 YxxΦ motifs. Mutation of Y108A in the YAWL motif at positions 108–111 disrupted GP3 sorting to downstream ER–Golgi intermediate compartments (ERGIC) and markedly reduced infectious virion production. In contrast, mutations in the YVDI motif did not alter GP3 trafficking patterns but exerted limited effects on viral replication, suggesting an indirect regulatory role. Interestingly, the ectopic monomeric expression of GP3-Y108A showed similar trafficking patterns to those of GP3-WT. These results provide novel insights into the molecular interplay between PRRSV envelope proteins and host trafficking machinery, contributing to a deeper understanding of PRRSV assembly, virion morphogenesis, and secretory dynamics. Our study also established LOIPA as a rapid and bacteria-free reverse genetics system for PRRSV, which is readily applicable to other member viruses in the family Arteriviridae , enabling functional interrogation of viral genes and rational engineering to produce mutant viruses.

  PublisherOA PDFDOI

• Swine TRIM25 restricts vesicular stomatitis virus replication by activating type I interferon signaling and binding viral RNA

  Journal of Veterinary Science · 2026-01-01

  articleOpen access

  Importance: Vesicular stomatitis virus is a zoonotic rhabdovirus that infects livestock and can cause economically important disease.Tripartite motif-containing 25 (TRIM25) is an E3 ubiquitin ligase involved in innate antiviral signaling, but its role in pigs during vesicular stomatitis virus infection is unclear.Objective: To define the mechanism by which swine TRIM25 restricts vesicular stomatitis virus replication.Methods: Porcine 3D4/21 cells with TRIM25 overexpression or knockdown were infected with vesicular stomatitis virus.Viral replication was quantified by immunoblotting, quantitative reverse transcription polymerase chain reaction, and 50% tissue culture infectious dose assays.Type I interferon signaling was assessed by transcript quantification, interferon-beta and interferon-stimulated response element reporter assays, and co-immunoprecipitation.Viral RNA binding was tested by RNA immunoprecipitation.Results: TRIM25 overexpression reduced viral RNA and infectious titers, whereas TRIM25 knockdown increased replication.TRIM25 increased interferon-beta and interferonstimulated gene expression and enhanced interferon-beta and interferon-stimulated response element promoter activity.Mechanistically, TRIM25 promoted Lys63-linked ubiquitination of RIG-I and increased phosphorylation of TANK-binding kinase 1 and interferon regulatory factor 3. TRIM25 also bound vesicular stomatitis virus genomic RNA, and binding required the C-terminal region.Conclusions and Relevance: Porcine TRIM25 restricts vesicular stomatitis virus replication by amplifying type I interferon signaling and directly binding viral RNA.

  PublisherOA PDFDOI

• Toward a better understanding of genetic diversity and more effective control strategies of major swine viral diseases

  Virology · 2025-03-01

  editorialCorresponding
  PublisherDOI

• Coinfection with bacterial pathogens and genetic modification of PRRSV-2 for suppression of NF-κB and attenuation of proinflammatory responses

  Virology · 2025-03-07 · 4 citations

  reviewOpen accessSenior authorCorresponding

  Porcine reproductive and respiratory syndrome virus (PRRSV) infects pulmonary alveolar macrophages and induces inflammation in the respiratory system. In swine farms, coinfection with PRRSV and bacterial pathogens is common and can result in clinically complicated outcomes, including porcine respiratory disease complex. Coinfection can cause excessive expressions of proinflammatory mediators and may lead to cytokine-storm-like syndrome. An immunological hallmark of PRRSV-2 is the bidirectional regulation of NF-κB with the nucleocapsid (N) protein identified as the NF-κB activator. We generated an NF-κB-silencing mutant PRRSV-2 by mutating the N gene to block its binding to PIAS1 [protein inhibitor of activated STAT-1 (signal transducer and activator of transcription 1)]. PIAS1 functions as an NF-κB repressor, and thus, the PIAS1-binding modified N-mutant PRRSV-2 became NF-κB activation-resistant in its phenotype. During coinfection of pigs with PRRSV-2 and Streptococcus suis , the N-mutant PRRSV-2 decreased the expression of proinflammatory cytokines and showed clinical attenuation. This review describes the coinfection of pigs with various pathogens, the generation of mutant PRRSV for NF-κB suppression, inflammatory profiles during bacterial coinfection, and the potential application of these findings to designing a new vaccine candidate for PRRSV-2. • Polymicrobial respiratory infection is common in pigs with increased clinical severity. • PRRSV infection activates NF-kB and coinfection causes overproduction of inflammatory cytokines. • PRRSV-mediated NF-kB activation can be modified to reduce inflammatory cytokines. • Using the P129 strain of PRRSV-2, 43 KK in the N protein has been mutated to 43 GG. • The N-mutant PRRSV is clinically attenuated during coinfection with Streptococcus suis.

  PublisherDOI

• The interplay between RNase L and the host cell or viruses: A review

  International Journal of Biological Macromolecules · 2025-12-28

  article
  PublisherDOI

• GTPase activity of porcine Mx1 plays a dominant role in inhibiting the N-Nsp9 interaction and thus inhibiting PRRSV replication

  Journal of Virology · 2024-03-04 · 9 citations

  articleOpen access

  Porcine Mx1 is a type of interferon-induced GTPase that inhibits the replication of certain RNA viruses. However, the antiviral effects and the underlying mechanism of porcine Mx1 for porcine reproductive and respiratory syndrome virus (PRRSV) remain unknown. In this study, we demonstrated that porcine Mx1 could significantly inhibit PRRSV replication in MARC-145 cells. By Mx1 segment analysis, it was indicated that the GTPase domain (68-341aa) was the functional area to inhibit PRRSV replication and that Mx1 interacted with the PRRSV-N protein through the GTPase domain (68-341aa) in the cytoplasm. Amino acid residues K295 and K299 in the G domain of Mx1 were the key sites for Mx1-N interaction while mutant proteins Mx1(K295A) and Mx1(K299A) still partially inhibited PRRSV replication. Furthermore, we found that the GTPase activity of Mx1 was dominant for Mx1 to inhibit PRRSV replication but was not essential for Mx1-N interaction. Finally, mechanistic studies demonstrated that the GTPase activity of Mx1 played a dominant role in inhibiting the N-Nsp9 interaction and that the interaction between Mx1 and N partially inhibited the N-Nsp9 interaction. We propose that the complete anti-PRRSV mechanism of porcine Mx1 contains a two-step process: Mx1 binds to the PRRSV-N protein and subsequently disrupts the N-Nsp9 interaction by a process requiring the GTPase activity of Mx1. Taken together, the results of our experiments describe for the first time a novel mechanism by which porcine Mx1 evolves to inhibit PRRSV replication. IMPORTANCE: Mx1 protein is a key mediator of the interferon-induced antiviral response against a wide range of viruses. How porcine Mx1 affects the replication of porcine reproductive and respiratory syndrome virus (PRRSV) and its biological function has not been studied. Here, we show that Mx1 protein inhibits PRRSV replication by interfering with N-Nsp9 interaction. Furthermore, the GTPase activity of porcine Mx1 plays a dominant role and the Mx1-N interaction plays an assistant role in this interference process. This study uncovers a novel mechanism evolved by porcine Mx1 to exert anti-PRRSV activities.

  PublisherOA PDFDOI

• Swine NONO promotes IRF3-mediated antiviral immune response by Detecting PRRSV N protein

  PLoS Pathogens · 2024-10-16 · 7 citations

  articleOpen accessCorresponding

  Non-POU domain-containing octamer-binding protein (NONO) is a multi-functional nuclear protein which belongs to the Drosophila behavior/human splicing (DBHS) protein family. NONO is known to regulate multiple important biological processes including host antiviral immune response. However, whether NONO can inhibit porcine reproductive and respiratory syndrome virus (PRRSV) replication is less well understood. In this study, we demonstrated that swine NONO (sNONO) inhibited PRRSV replication, via increasing expression of IFN-β, whereas NONO knockdown or knockout in PAM-KNU cells was more susceptible to PRRSV infection. As an IRF3 positive regulation factor, NONO promoted IFN-β expression by enhancing activation of IRF3. During PRRSV infection, NONO further up-regulated IRF3-mediated IFN-β expression by interacting with PRRSV N protein. Mechanistically, NONO functioned as a scaffold protein to detect PRRSV N protein and formed N-NONO-IRF3 complex in the nucleus. Interestingly, it was found that the NONO protein reversed the inhibitory effect of PRRSV N protein on type I IFN signaling pathway. Taken together, our study provides a novel mechanism for NONO to increase the IRF3-mediated IFN-β activation by interacting with the viral N protein to inhibit PRRSV infection.

  PublisherDOI

• A clinically attenuated double-mutant of porcine reproductive and respiratory syndrome virus-2 that does not prompt overexpression of proinflammatory cytokines during co-infection with a secondary pathogen

  PLoS Pathogens · 2024-03-28 · 11 citations

  articleOpen accessSenior authorCorresponding

  Porcine reproductive and respiratory syndrome virus (PRRSV) is known to suppress the type I interferon (IFNs-α/β) response during infection. PRRSV also activates the NF-κB signaling pathway, leading to the production of proinflammatory cytokines during infection. In swine farms, co-infections of PRRSV and other secondary bacterial pathogens are common and exacerbate the production of proinflammatory cytokines, contributing to the porcine respiratory disease complex (PRDC) which is clinically a severe disease. Previous studies identified the non-structural protein 1β (nsp1β) of PRRSV-2 as an IFN antagonist and the nucleocapsid (N) protein as the NF-κB activator. Further studies showed the leucine at position 126 (L126) of nsp1β as the essential residue for IFN suppression and the region spanning the nuclear localization signal (NLS) of N as the NF-κB activation domain. In the present study, we generated a double-mutant PRRSV-2 that contained the L126A mutation in the nsp1β gene and the NLS mutation (ΔNLS) in the N gene using reverse genetics. The immunological phenotype of this mutant PRRSV-2 was examined in porcine alveolar macrophages (PAMs) in vitro and in young pigs in vivo. In PAMs, the double-mutant virus did not suppress IFN-β expression but decreased the NF-κB-dependent inflammatory cytokine productions compared to those for wild-type PRRSV-2. Co-infection of PAMs with the mutant PRRSV-2 and Streptococcus suis (S. suis) also reduced the production of NF-κB-directed inflammatory cytokines. To further examine the cytokine profiles and the disease severity by the mutant virus in natural host animals, 6 groups of pigs, 7 animals per group, were used for co-infection with the mutant PRRSV-2 and S. suis. The double-mutant PRRSV-2 was clinically attenuated, and the expressions of proinflammatory cytokines and chemokines were significantly reduced in pigs after bacterial co-infection. Compared to the wild-type PRRSV-2 and S. suis co-infection control, pigs coinfected with the double-mutant PRRSV-2 exhibited milder clinical signs, lower titers and shorter duration of viremia, and lower expression of proinflammatory cytokines. In conclusion, our study demonstrates that genetic modification of the type I IFN suppression and NF-κB activation functions of PRRSV-2 may allow us to design a novel vaccine candidate to alleviate the clinical severity of PRRS-2 and PRDC during bacterial co-infection.

  PublisherOA PDFDOI

• Genomic RNA recombination of porcine reproductive and respiratory syndrome virus and other arteriviruses

  Virology · 2024-11-04 · 9 citations

  reviewOpen accessSenior authorCorresponding

  Arteriviruses in the Nidovirales order are single-stranded positive-sense RNA viruses infecting mammals. Arteriviruses are recognized for causing various clinical diseases, ranging from asymptomatic infections to severe conditions like respiratory syndromes and viral hemorrhagic fever. Notably, arteriviruses exhibit a high frequency of RNA recombination, and their robust recombination rates are a crucial factor in recurrent outbreaks. The recombination events also shape the countermeasures employed by arteriviruses during virus-host co-evolution and confer specific evolutionary benefits to viruses, implicating a role as a selective advantage in viral adaptation. This review delves into the molecular basis of RNA recombination in arteriviruses, the bioinformatics tools and methodologies used to visualize evolutionary relationships, and the identification of recombination breakpoints. Significant recombination events are highlighted for PRRSV and other arteriviruses, illustrating the profound implications of recombination for viral evolution and pathogenesis. Recombination between field viruses and between field viruses and vaccine strains can generate new variants with altered antigenic profiles and virulence, leading to diagnostic failure, severe clinical outcomes, and reduced vaccine efficacy. Despite the advances, further research is needed to understand recombination rates and hotspots, as well as to develop potential antiviral strategies and diagnostic approaches for arteriviruses.

  PublisherDOI

• Suppression of TRIM19 by arterivirus nonstructural protein 1 promotes viral replication

  Virus Research · 2023-12-21 · 3 citations

  articleOpen accessSenior authorCorresponding

  Tripartite motif (TRIM)-containing proteins are a family of regulatory proteins that can participate in the induction of antiviral cytokines and antagonize viral replication. Promyelocytic leukemia (PML) protein is known as TRIM19 and is a major scaffold protein organizing the PML nuclear bodies (NBs). PML NBs are membrane-less organelles in the nucleus and play a diverse role in maintaining cellular homeostasis including antiviral response. Porcine reproductive and respiratory syndrome virus (PRRSV), a member virus of the family Arteriviridae, inhibits type I interferon (IFN) response during infection, and nonstructural protein 1 (nsp1) of the virus has been identified as a potent IFN antagonist. We report that the numbers of PML NBs per nucleus were significantly downregulated during infection of PRRSV. The overexpression of all six isoforms of PML suppressed the PRRSV replication, and conversely, the silencing of PML gene expression enhanced the PRRSV replication. The suppression of PML NBs by the nsp1 protein was common in other member viruses of the family, represented by equine arteritis virus, lactate dehydrogenase elevating virus of mice, and simian hemorrhagic fever virus. Our study unveils a conserved viral strategy in arteriviruses for innate immune evasion.

  PublisherDOI

Frequent coauthors

• Lorne A. Babiuk

  University of Alberta

  20 shared

• Yijun Du

  Shandong Academy of Agricultural Sciences

  18 shared

• Davor Ojkić

  University of Guelph

  14 shared

• John R. Barta

  University of Guelph

  14 shared

• Changhee Lee

  New Generation University College

  14 shared

• Mingyuan Han

  13 shared

• Maged Gomaa

  10 shared

• Raymond R. R. Rowland

  University of Illinois Urbana-Champaign

  10 shared

Labs

• Pathobiology Department of Pathobiology, College of Veterinary MedicinePI

Education

• PhD, Microbiology and Immunology

  University of Ottawa Faculty of Medicine

• MSc

  Seoul National University

• DVM

  Seoul National University

Awards & honors

• Gordon and Helen Kruger Research Excellence Award (2018)
• Pfizer Award for Research Excellence (2012)
• Pfizer Faculty Award for Research Excellence (2003)
• Presidential Distinguished Professor Award (Research) (2003)