Supplementation of oil-based inactivated H9N2 vaccine with M2e antigen enhances resistance against heterologous H9N2 avian influenza virus infection

Park, J.K.,Lee, D.H.,Cho, C.H.,Yuk, S.S.,To, E.O.,Kwon, J.H.,Noh, J.Y.,Kim, B.Y.,Choi, S.W.,Shim, B.S.,Song, M.K.,Lee, J.B.,Park, S.Y.,Choi, I.S.,Song, C.S. Elsevier Scientific Pub. Co 2014 Veterinary microbiology Vol.169 No.3

Avian influenza virus (AIV) subtype H9N2 has been evolving rapidly and vaccine escape variants have been reported to cause circulation of infections and economic losses. In the present study, we developed and evaluated ectodomain of the AIV matrix 2 (M2e) protein as a supplementing antigen for oil-based inactivated H9N2 vaccine to increase resistance against vaccine escape variants. AIV H9N2 M2e antigen was expressed in Escherichia coli and supplemented to inactivated H9N2 oil emulsion vaccine. Specific pathogen-free chickens received a single injection of inactivated H9N2 oil emulsion vaccines with or without M2e supplementation. At three weeks post vaccination, hemagglutination inhibition tests and enzyme-linked immunosorbent assays were performed to determine serological immune responses. Challenge study using a vaccine escape H9N2 variant was performed to evaluate the efficacy of M2e supplementation. M2e antigen supplemented in oil emulsion vaccine was highly immunogenic, and a single M2e-supplemented vaccination reduced challenge virus replication and shedding more effectively than non-supplemented vaccination.

Evaluation of the zoonotic potential of a novel reassortant H1N2 swine influenza virus with gene constellation derived from multiple viral sources

Lee, J.H.,Pascua, P.N.Q.,Decano, A.G.,Kim, S.M.,Park, S.J.,Kwon, H.I.,Kim, E.H.,Kim, Y.I.,Kim, H.,Kim, S.Y.,Song, M.S.,Jang, H.K.,Park, B.K.,Choi, Y.K. Elsevier Science 2015 INFECTION GENETICS AND EVOLUTION Vol.34 No.-

In 2011-2012, contemporary North American-like H3N2 swine influenza viruses (SIVs) possessing the 2009 pandemic H1N1 matrix gene (H3N2pM-like virus) were detected in domestic pigs of South Korea where H1N2 SIV strains are endemic. More recently, we isolated novel reassortant H1N2 SIVs bearing the Eurasian avian-like swine H1-like hemagglutinin and Korean swine H1N2-like neuraminidase in the internal gene backbone of the H3N2pM-like virus. In the present study, we clearly provide evidence on the genetic origins of the novel H1N2 SIVs virus through genetic and phylogenetic analyses. In vitro studies demonstrated that, in comparison with a pre-existing 2012 Korean H1N2 SIV [A/swine/Korea/CY03-1½012 (CY03-1½012)], the 2013 novel reassortant H1N2 isolate [A/swine/Korea/CY0423/2013 (CY0423-12/2013)] replicated more efficiently in differentiated primary human bronchial epithelial cells. The CY0423-12/2013 virus induced higher viral titers than the CY03-1½012 virus in the lungs and nasal turbinates of infected mice and nasal wash samples of ferrets. Moreover, the 2013 H1N2 reassortant, but not the intact 2012 H1N2 virus, was transmissible to naive contact ferrets via respiratory-droplets. Noting that the viral precursors have the ability to infect humans, our findings highlight the potential threat of a novel reassortant H1N2 SIV to public health and underscore the need to further strengthen influenza surveillance strategies worldwide, including swine populations.

Genetic and phylogenetic characterizations of a novel genotype of highly pathogenic avian influenza (HPAI) H5N8 viruses in 2016/2017 in South Korea

Kim, Y.I.,Park, S.J.,Kwon, H.I.,Kim, E.H.,Si, Y.J.,Jeong, J.H.,Lee, I.W.,Nguyen, H.D.,Kwon, J.J.,Choi, W.S.,Song, M.S.,Kim, C.J.,Choi, Y.K. Elsevier Science 2017 INFECTION GENETICS AND EVOLUTION Vol.53 No.-

<P>During the outbreaks of highly pathogenic avian influenza (HPAI) H5N6 viruses in 2016 in South Korea, novel H5N8 viruses were also isolated from migratory birds. Phylogenetic analysis revealed that the HA gene of these H5N8 viruses belonged to clade 2.3.4.4, similarly to recent H5Nx viruses, and originated from A/Brk/Korea/Gochang1/14(H5N8), a minor lineage of H5N8 that appeared in 2014 and then disappeared. At least four reassortment events occurred with different subtypes (H5N8, H7N7, H3N8 and H10N7) and a chicken challenge study revealed that they were classified as HPAI viruses according to OIE criteria. (C) 2017 Elsevier B.V. All rights reserved.</P>

Cross-protective efficacies of highly-pathogenic avian influenza H5N1 vaccines against a recent H5N8 virus

Park, S.J.,Si, Y.J.,Kim, J.,Song, M.S.,Kim, S.m.,Kim, E.H.,Kwon, H.i.,Kim, Y.I.,Lee, O.J.,Shin, O.S.,Kim, C.J.,Shin, E.C.,Choi, Y.K. Academic Press 2016 Virology Vol.498 No.-

<P>To investigate cross-protective vaccine efficacy of highly-pathogenic avian influenza H5N1 viruses against a recent HPAI H5N8 virus, we immunized C57BL/6 mice and ferrets with three alum-adjuvanted inactivated whole H5N1 vaccines developed through reverse-genetics (Rg): [Vietnam/1194/04xPR8 (clade 1), Korea/W149/06xPR8 (clade 2.2), and Korea/ES223N/03xPR8 (clade 2.5)]. Although relatively low cross-reactivities (10-40 HI titer) were observed against heterologous H5N8 virus, immunized animals were 100% protected from challenge with the 20 mLD(50) of H5N8 virus, with the exception of mice vaccinated with 3.5 mu g of Rg Vietnam/1194/04xPR8. Of note, the Rg Korea/ES223N/03xPR8 vaccine provided not only effective protection, but also markedly inhibited viral replication in the lungs and nasal swabs of vaccine recipients within five days of HPAI H5N8 virus challenge. Further, we demonstrated that antibody-dependent cell-mediated cytotoxicity (ADCC) of an antibody-coated target cell by cytotoxic effector cells also plays a role in the heterologous protection of H5N1 vaccines against H5N8 challenge. (C) 2016 Elsevier Inc. All rights reserved.</P>

Peroxiredoxin II promotes hepatic tumorigenesis through cooperation with Ras/Forkhead box M1 signaling pathway

Park, Y-H,Kim, S-U,Kwon, T-H,Kim, J-M,Song, I-S,Shin, H-J,Lee, B-K,Bang, D-H,Lee, S-J,Lee, D-S,Chang, K-T,Kim, B-Y,Yu, D-Y Macmillan Publishers Limited 2016 Oncogene Vol.35 No.27

<P>The current study was carried out to define the involvement of Peroxiredoxin (Prx) II in progression of hepatocellular carcinoma (HCC) and the underlying molecular mechanism(s). Expression and function of Prx II in HCC was determined using H-ras(G12V)-transformed HCC cells (H-ras(G12V)-HCC cells) and the tumor livers from H-ras(G12V)-transgenic (Tg) mice and HCC patients. Prx II was upregulated in H-ras(G12V)-HCC cells and H-ras(G12V)-Tg mouse tumor livers, the expression pattern of which highly similar to that of forkhead Box M1 (FoxM1). Moreover, either knockdown of FoxM1 or site-directed mutagenesis of FoxM1-binding site of Prx II promoter significantly reduced Prx II levels in H-ras(G12V)-HCC cells, indicating FoxM1 as a direct transcription factor of Prx II in HCC. Interestingly, the null mutation of Prx II markedly decreased the number and size of tumors in H-ras(G12V)-Tg livers. Consistent with this, knockdown of Prx II in H-ras(G12V)-HCC cells reduced the expression of cyclin D1, cell proliferation, anchorage-independent growth and tumor formation in athymic nude mice, whereas overexpression of Prx II increased or aggravated the tumor phenotypes. Importantly, the expression of Prx II was correlated with that of FoxM1 in HCC patients. The activation of extracellular signal-related kinase (ERK) pathway and the expression of FoxM1 and cyclin D1 were highly dependent on Prx II in H-ras(G12V)-HCC cells and H-ras(G12V)-Tg livers. Prx II is FoxM1-dependently- expressed antioxidant in HCC and function as an enhancer of Ras(G12V) oncogenic potential in hepatic tumorigenesis through activation of ERK/FoxM1/cyclin D1 cascade.</P>

냉축열을 위한 H₂O-NaCl 혼합물의 상변화 온도와 잠열 특성분석

송현갑(H.K.Song),노정근(J.G.Ro) 한국태양에너지학회 1999 한국태양에너지학회 논문집 Vol.19 No.2

H₂0-NaCl혼합물을 냉축열재로 선택하였으며, 이 혼합물의 상변화온도를 몰농도 변화에 의하여 조절하였다. 그리고 고농도와 저농도의 NaCl과 H₂0가 ion-dipole interaction으로 결합하는 구조를 그림으로 가시화하고 가열, 냉각과정에서 H₂0-NaCl이 동결, 융해하는 현상을 도시하므로서 융해와 동결과정에서 상변화온도가 2단계로 나타나는 구조적 원인을 구명하였으며, NaCl의 농도변화에 따른 상변화온도를 이론적으로 분석하므로서 실험 및 이론분석 결과의 타당성을 증명할 수 있도록 하였다. In this study H₂0-NaCl mixture was selected as a cold thermal storage material and its phase change temperature(liquid>solid) was controlled with the molar concentration of NaCl.<br/> Ion dipole interaction mechanism and the fusion and crystallization structure of H₂O-NaCl were visualized' with the low and high concentration of NaCl in the heating and cooling processes.<br/> In this study, the original cause of the appearance of two steps phase change period in heating and cooing processes were found by the visualization of the ion dipole interaction mechanism of H₂O- NaCl, and the theoretical equation of the phase change temperature variation in the NaCl high molar concentration was rearranged.

Biological evaluation of anti-influenza viral activity of semi-synthetic catechin derivatives

Song, J.M.,Park, K.D.,Lee, K.H.,Byun, Y.H.,Park, J.H.,Kim, S.H.,Kim, J.H.,Seong, B.L. Elsevier/North-Holland 2007 ANTIVIRAL RESEARCH Vol.76 No.2

Catechin derivatives with different alkyl chain length and aromatic ring substitutions at the 3-hydroxyl group were synthesized from epigallocatechin (EGC) and (+)-catechin (C) and their anti-influenza viral activity were evaluated in vitro and in ovo. Pronounced antiviral activity was observed for derivatives carrying moderate chain length (7-9 carbons) as compared to those with aromatic rings, whereas the 5'-hydroxyl group of the trihydroxy benzyl moiety did not significantly contribute to antiviral activity. The derivatives exerted inhibitory effects for all six influenza subtypes tested including three major types of currently circulating human influenza viruses (A/H1N1, A/H3N2 and B type), H2N2 and H9N2 avian influenza virus. The compounds strongly inhibited adsorption of the viruses on red blood cell (RBC). They also restricted the growth of avian influenza virus in ovo with minimum inhibition concentration (MIC) of 5-10μM far exceeding the neuraminidase (NA) inhibitor oseltamivir or M2 proton channel inhibitor amantadine. The antiviral activity appears to be mediated by interaction with hemagglutinin (HA)/viral membrane rendering HA less fusogenic at the initial stage of infection. The broad spectrum activity against various subtypes of influenza viruses may complement the limitations of current antivirals and contribute for managing potentially emerging influenza pandemic. The structure-activity data of catechin derivatives may usefully guideline future research endeavors for applying green tea catechins as alternative anti-viral agents.

Evidence of Human-to-Swine Transmission of the Pandemic (H1N1) 2009 Influenza Virus in South Korea

Song, M.-S.,Lee, J. H.,Pascua, P. N. Q.,Baek, Y. H.,Kwon, H.-i.,Park, K. J.,Choi, H.-W.,Shin, Y.-K.,Song, J.-Y.,Kim, C.-J.,Choi, Y.-K. American Society for Microbiology 2010 Journal of clinical microbiology Vol.48 No.9

냉축열을 위한 H₂O - NaCl 혼합물의 상변화 온도와 잠열 특성분석

송현갑(H. K. Song),노정근(J. G. Ro) 한국태양에너지학회 1999 한국태양에너지학회 학술대회논문집 Vol.- No.-

H₂O-NaCl혼합물을 냉축열재로 선택하였으며, 이 혼합물의 상변온도를 물농도 변화에 의하여 조절하였다. 그리고 고농도와 저농도의 NaCl과 H₂O가 Ion-dipole interaction으로 결합하는 구조를 그림으로 가시화하고 가열, 냉각과정에서 H₂O-NaCl이 동결, 융해하는 현상을 도시하므로서 융해와 동결과정에서 상변화온도가 2단계로 나타나는 구조적 원인을 구명하였으며, NaCl의 농도변화에 따른 상변온도를 이론적으로 분석하므로서 실험 및 이론분석 결과의 타당성을 증명할 수 있도록 하였다. In this study H₂O-NaCl mixture was selected as the thermal storage material and it's phase change temperature(liquid⇔solid) was controlled with the molar concentration of Nacl.<br/> Ion dipole interaction mechanism and the fusion and crystallization structure of H₂O-NaCl were visualized with the low and high concentration of NaCl in the heating and cooling processes.<br/> The original cause of the appearance of two steps phase change period in each process was found by the visualization of the ion dipole interaction mechanism of H₂O-NaCl, and the theoretical model of the phase change temperature variation with the NaCl molar concentration was developed.

Pathogenicity and transmission studies of H7N7 avian influenza virus isolated from feces of magpie origin in chickens and magpie

Kim, M.C.,Jeong, O.M.,Kang, H.M.,Paek, M.R.,Kwon, J.S.,Song, C.S.,Kwon, Y.K.,Lee, J.G.,Kwon, J.H.,Lee, Y.J. Elsevier Scientific Pub. Co 2010 Veterinary microbiology Vol.141 No.3

An H7N7 avian influenza virus [A/Magpie/Kr/YJD174/07 (H7N7); Mp/Kr/07 virus] was isolated from magpie feces in the north-western area (Youngjongdo) of South Korea and identified as low pathogenicity by intravenous pathogenic index and amino acid sequence of cleavage site. In genetic analysis, the genome of the Mp/Kr/07 virus was the same as those of two other H7N7 viruses isolated from the Mallard ducks in Ganghwa, 5km north of Youngjongdo, and grouped under the H7-subtype Eurasian linage with the highest similarity to recent two domestic duck isolates in South Korea. In vivo studies of the chickens and magpies, the Mp/Kr/07 virus, though did not caused any clinical signs with histological changes, could replicate in the oropharynx and cloaca of the chickens and was efficiently transmitted to contact chickens. However, the virus was restrictively identified in oropharynx of the magpies and was not spread to magpies by direct contact. These results suggest that magpie are not a biological amplifier of influenza virus and thus play a minimal role in virus transmission as intermediate host.