http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Kim, Deok-Song,Hosmillo, Myra,Alfajaro, Mia Madel,Kim, Ji-Yun,Park, Jun-Gyu,Son, Kyu-Yeol,Ryu, Eun-Hye,Sorgeloos, Frederic,Kwon, Hyung-Jun,Park, Su-Jin,Lee, Woo Song,Cho, Duck,Kwon, Joseph,Choi, Jong- Public Library of Science 2014 PLoS pathogens Vol.10 No.6
<▼1><P>Sapovirus, a member of the <I>Caliciviridae</I> family, is an important cause of acute gastroenteritis in humans and pigs. Currently, the porcine sapovirus (PSaV) Cowden strain remains the only cultivable member of the <I>Sapovirus</I> genus. While some caliciviruses are known to utilize carbohydrate receptors for entry and infection, a functional receptor for sapovirus is unknown. To characterize the functional receptor of the Cowden strain of PSaV, we undertook a comprehensive series of protein-ligand biochemical assays in mock and PSaV-infected cell culture and/or piglet intestinal tissue sections. PSaV revealed neither hemagglutination activity with red blood cells from any species nor binding activity to synthetic histo-blood group antigens, indicating that PSaV does not use histo-blood group antigens as receptors. Attachment and infection of PSaV were markedly blocked by sialic acid and <I>Vibrio cholerae</I> neuraminidase (NA), suggesting a role for α2,3-linked, α2,6-linked or α2,8-linked sialic acid in virus attachment. However, viral attachment and infection were only partially inhibited by treatment of cells with sialidase S (SS) or <I>Maackia amurensis</I> lectin (MAL), both specific for α2,3-linked sialic acid, or <I>Sambucus nigra</I> lectin (SNL), specific for α2,6-linked sialic acid. These results indicated that PSaV recognizes both α2,3- and α2,6-linked sialic acids for viral attachment and infection. Treatment of cells with proteases or with benzyl 4-O-β-D-galactopyranosyl-β-D-glucopyranoside (benzylGalNAc), which inhibits <I>O</I>-linked glycosylation, also reduced virus binding and infection, whereas inhibition of glycolipd synthesis or <I>N</I>-linked glycosylation had no such effect on virus binding or infection. These data suggest PSaV binds to cellular receptors that consist of α2,3- and α2,6-linked sialic acids on glycoproteins attached via <I>O</I>-linked glycosylation.</P></▼1><▼2><P><B>Author Summary</B></P><P>Although enteropathogenic sapoviruses and noroviruses are leading causes of acute gastroenteritis in both humans and animals, the study of viral pathogenesis and immunity of these ubiquitous pathogens has been hampered due to the lack of a fully permissive cell culture system. Porcine sapovirus Cowden strain provides a suitable system that can be used to identify the molecular mechanisms of viral pathogenesis. Previous studies have shown that carbohydrates and glycolipids play important roles in the attachment of members of the <I>Caliciviridae</I>; histo-blood group antigens (HBGAs) are used by <I>Norovirus</I> genogroups I to IV, as well as members of the <I>Lagovirus</I>, and <I>Recovirus</I> genera, whereas terminal sialic acid is recognized as a receptor for feline calicivirus and murine norovirus. To date, however, the role of carbohydrates in the life cycle of sapoviruses has remained largely unknown. We found that porcine sapovirus binds to susceptible host cells through both α2,3- and α2,6-linked terminal sialic acids which are attached to <I>O</I>-linked glycoproteins. These efforts, findings and insights will significantly contribute to a better understanding of the sapovirus life cycle.</P></▼2>
Glycan-specificity of four neuraminidase-sensitive animal rotavirus strains
Kim, Ji-Yun,Kim, Deok-Song,Seo, Ja-Young,Park, Jun-Gyu,Alfajaro, Mia Madel,Soliman, Mahmoud,Baek, Yeong-Bin,Cho, Eun-Hyo,Kwon, Hyung-Jun,Park, Su-Jin,Kang, Mun-Il,Cho, Kyoung-Oh Elsevier Scientific Pub. Co 2017 Veterinary microbiology Vol.207 No.-
<P><B>Abstract</B></P> <P>Group A rotaviruses (RVAs) are divided into neuraminidase (NA)-sensitive and NA-insensitive strains depending upon their binding affinity to the VP8* domain in the terminal sialic acids (SAs) of cell surface carbohydrates. Although NA-sensitive strains are known to use terminal SAs as an attachment factor, the exact nature of this attachment factor is largely unknown. Here we show that the specific linkage of SA-containing glycan to glycoprotein or glycolipid is an attachment factor used by NA-sensitive porcine G9P[7] PRG9121 and G9P[23] PRG942, bovine G6P[1] NCDV, and canine G3P[3] strains. Infectivity of porcine G9P[7] and G9P[23] strains was markedly blocked by α2,3-linkage and α2,6-linkage inhibitors, indicating that these strains bind to both α2,3- and α2,6-linked SAs. However, the infectivity of bovine G6P[1] and canine G3P[3] strains was significantly reduced by α2,6-linkage inhibitor but not by α2,3-linkage blockers, demonstrating a predilection of these strains for α2,6-linked SAs. The infectivity of four NA-sensitive strains was equally reduced by inhibitors of lipid membrane and <I>N</I>-linked glycoprotein but not by an inhibitor of <I>O</I>-linked glycoprotein, indicating that these strains utilize both glycolipid and <I>N</I>-linked glycoprotein. Our study demonstrates that four NA-sensitive animal strains could have a strain-dependent binding preference toward α2,6-linked SAs (P[1] NCDV and P[3] CU-1 strains) or both α2,3- and α2,6-linked SAs (P[7] PRG9121 and P[23] PRG942 strains) to the glycolipid and <I>N</I>-linked glycoprotein.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Porcine P[7] and P[23] strains use α2,3- and α2,6-linked SAs as receptors. </LI> <LI> Bovine P[1] and canine P[3] strains bind α2,6-linked SAs as receptors. </LI> <LI> These strains use SAs on glycolipid and N-linked glycoprotein as receptors. </LI> </UL> </P>
Park, Jun-Gyu,Kim, Hyun-Jeong,Matthijnssens, Jelle,Alfajaro, Mia Madel,Kim, Deok-Song,Son, Kyu-Yeol,Kwon, Hyoung-Jun,Hosmillo, Myra,Ryu, Eun-Hye,Kim, Ji-Yun,Cena, Rohani B,Lee, Ju-Hwan,Kang, Mun-Il,Pa BioMed Central 2013 Veterinary research Vol.44 No.-
<P>Direct interspecies transmissions of group A rotaviruses (RVA) have been reported under natural conditions. However, the pathogenicity of RVA has never been directly compared in homologous and heterologous hosts. The bovine RVA/Cow-tc/KOR/K5/2004/G5P[7] strain, which was shown to possess a typical porcine-like genotype constellation similar to that of the G5P[7] prototype RVA/Pig-tc/USA/OSU/1977/G5P9[7] strain, was examined for its pathogenicity and compared with the porcine G5P[7] RVA/Pig-tc/KOR/K71/2006/G5P[7] strain possessing the same genotype constellation. The bovine K5 strain induced diarrhea and histopathological changes in the small intestine of piglets and calves, whereas the porcine K71 strain caused diarrhea and histopathological changes in the small intestine of piglets, but not in calves. Furthermore, the bovine K5 strain showed extra-intestinal tropisms in both piglets and calves, whereas the porcine K71 strain had extra-intestinal tropisms in piglets, but not in calves. Therefore, we performed comparative genomic analysis of the K71 and K5 RVA strains to determine whether specific mutations could be associated with these distinct clinical and pathological phenotypes. Full-length sequencing analyses for the 11 genomic segments for K71 and K5 revealed that these strains were genetically nearly identical to each other. Two nucleotide mutations were found in the 5′ untranslated region (UTR) of NSP5 and the 3′ UTR of NSP3, and eight amino acid mutations in VP1-VP4 and NSP2. Some of these mutations may be critical molecular determinants for RVA virulence and/or pathogenicity.</P>
Molecular epidemiology of Korean porcine sapeloviruses
Son, Kyu-Yeol,Kim, Deok-Song,Matthijnssens, Jelle,Kwon, Hyoung-Jun,Park, Jun-Gyu,Hosmillo, Myra,Alfajaro, Mia Madel,Ryu, Eun-Hye,Kim, Ji-Yun,Kang, Mun-Il,Cho, Kyoung-Oh Springer-Verlag 2014 Archives of virology Vol.159 No.5
<P>To evaluate the prevalence and genetic diversity of porcine sapeloviruses (PSVs) in Korea, a total of 100 diarrhea fecal samples from pigs were analyzed by RT-PCR and nested PCR assays with primer pairs specific for the VP1 gene. Overall, 34 % of the diarrhea samples tested positive for PSV, and a high proportion of infections occurred along with a variety of other enteric viruses and bacteria. Genomic and phylogenetic analysis of the VP1 genes revealed pronounced genetic diversities between PSVs from Korean and elsewhere. Our results indicate that PSV infections are very common in Korean pigs with diarrhea. The infecting strains are genetically diverse.</P>
Whole genomic characterization of Korean porcine G8P[7] reassortant rotaviruses
Park, Jun-Gyu,Park, Sang-Ik,Woo, Nam-Il,Kim, Deok-Song,Seo, Ja-Young,Alfajaro, Mia Madel,Kim, Ji-Yun,Soliman, Mahmoud,Baek, Yeong-Bin,Cho, Eun-Hyo,Kwon, Joseph,Choi, Jong-Soon,Kang, Mun-Il,Matthijnsse Springer-Verlag 2016 Archives of virology Vol.161 No.10
<P>This study analyzed eleven genomic segments of three Korean porcine G8P[7] group A rotavirus (RVA) strains. Phylogenetically, these strains contained two bovine-like and nine porcine-like genomic segments. Eight genes (VP1, VP2, VP6 and NSP1-NSP5) of strains 156-1 and 42-1 and seven genes (VP1, VP2, VP6 and NSP2-NSP5) of strain C-1 clustered closely with porcine and porcine-like animal strains and distantly from typical human Wa-like strains. The VP3-M2 genotype of these strains clustered closely with bovine-like strains, but distantly with typical human DS-1-like strains. These data indicate that multiple reassortments involving porcine and bovine RVA strains in Korea must have occurred.</P>
Soliman, Mahmoud,Seo, Ja-Young,Kim, Deok-Song,Kim, Ji-Yun,Park, Jun-Gyu,Alfajaro, Mia Madel,Baek, Yeong-Bin,Cho, Eun-Hyo,Kwon, Joseph,Choi, Jong-Soon,Kang, Mun-Il,Park, Sang-Ik,Cho, Kyoung-Oh Public Library of Science 2018 PLoS pathogens Vol.14 No.1
<▼1><P>The cellular PI3K/Akt and/or MEK/ERK signaling pathways mediate the entry process or endosomal acidification during infection of many viruses. However, their roles in the early infection events of group A rotaviruses (RVAs) have remained elusive. Here, we show that late-penetration (L-P) human DS<I>-</I>1 and bovine NCDV RVA strains stimulate these signaling pathways very early in the infection. Inhibition of both signaling pathways significantly reduced production of viral progeny due to blockage of virus particles in the late endosome, indicating that neither of the two signaling pathways is involved in virus trafficking. However, immunoprecipitation assays using antibodies specific for pPI3K, pAkt, pERK and the subunit E of the V-ATPase co-immunoprecipitated the V-ATPase in complex with pPI3K, pAkt, and pERK. Moreover, Duolink proximity ligation assay revealed direct association of the subunit E of the V-ATPase with the molecules pPI3K, pAkt, and pERK, indicating that both signaling pathways are involved in V-ATPase-dependent endosomal acidification. Acidic replenishment of the medium restored uncoating of the RVA strains in cells pretreated with inhibitors specific for both signaling pathways, confirming the above results. Isolated components of the outer capsid proteins, expressed as VP4-VP8* and VP4-VP5* domains, and VP7, activated the PI3K/Akt and MEK/ERK pathways. Furthermore, psoralen-UV-inactivated RVA and CsCl-purified RVA triple-layered particles triggered activation of the PI3K/Akt and MEK/ERK pathways, confirming the above results. Our data demonstrate that multistep binding of outer capsid proteins of L-P RVA strains with cell surface receptors phosphorylates PI3K, Akt, and ERK, which in turn directly interact with the subunit E of the V-ATPase to acidify the late endosome for uncoating of RVAs. This study provides a better understanding of the RVA<I>-</I>host interaction during viral uncoating, which is of importance for the development of strategies aiming at controlling or preventing RVA infections.</P></▼1><▼2><P><B>Author summary</B></P><P>Viral particles must transport their genome into the cytoplasm or the nucleus of host cells to initiate successful infection. Knowledge of how viruses may pirate host cell signaling cascades or molecules to promote their own replication can facilitate the development of antiviral drugs. Group A rotavirus (RVA) is a major etiological agent of acute gastroenteritis in young children and the young of various mammals. RVA enters cells by a complex multistep process. However, the cellular signaling cascades or molecules that facilitate these processes are incompletely understood. Here, we demonstrate that infection with late-penetration RVA strains results in phosphorylation of PI3K, Akt, and ERK signaling molecules at an early stage of infection, a process mediated by the multistep binding of RVAs outer capsid proteins. Specific inhibitors for PI3K/Akt and MEK/ERK signaling pathways trap the viral particles in late endosome, and acidic replenishment restores and releases them. Moreover, the RVA-induced phosphorylated PI3K, Akt, and ERK directly interact with the subunit E of the V-ATPase proton pump, required for endosomal acidification and RVA uncoating. Understanding how RVA-induced early activation of cellular signaling molecules mediates the V-ATPase-dependent endosomal acidification required for uncoating of viral particles opens up opportunities for targeted interventions against rotavirus entry.</P></▼2>
Molecular detection of genotype 3 porcine hepatitis E virus in aborted fetuses and their sows
Hosmillo, Myra,Jeong, Young-Ju,Kim, Hyun-Jeong,Park, Jun-Gyu,Nayak, Mukti Kant,Alfajaro, Mia Madel,Collantes, Therese Marie,Park, Su-Jin,Ikuta, Kazuyoshi,Yunoki, Mikihiro,Kang, Mun-Il,Park, Sang-Ik,Ch Springer-Verlag 2010 Archives of virology Vol.155 No.7