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Kang-seuk Choi,Jin-ju Nah,Young-joon Ko,Shien-young Kang,Yi-seol Joo 대한수의학회 2003 Journal of Veterinary Science Vol.4 No.2
of Antigenic Sites at the Amino-terminus of Rinderpest Virus N Protein Using Deleted N Mutants and Monoclonal AntibodyKang-seuk Choi*, Jin-ju Nah, Young-joon Ko, Shien-young Kang1 and Yi-seok JooNational Veterinary Research and Quarantine service, Ministry of Agriculture and Forestry, 480 Anyang, Gyounggi 430-824, Korea1Research Institute of Veterinary Medicine, College of Veterinary Medicine, Chungbuk National University, 48 Gaeshin-dong, Heungduk-gu, Cheongju, Chungbuk 361-763, KoreaReceived April 2, 2003 / Accept July 10, 2003J. Vet. Sci. (2003), 4(2), 167-173JOURNAL OFVeterinaryScience*Corresponding author: Kang-seuk Choi National Veterinary Research and Quarantine service, Ministry of Agriculture and Forestry, 480 Anyang, Gyounggi 430-824, Korea Tel: +82-31-467-1860, Fax: +82-31-449-5882 E-mail: choiks@nvrqs.go.kr
Genetic diversity of avian paramyxovirus type 4 isolates from wild ducks in Korea from 2006 to 2011.
Choi, Kang-Seuk,Kim, Ji-Ye,Kye, Soo-Jeong,Park, Choi-Kyu,Sung, Haan-Woo M. Nijhoff ; Kluwer Academic Publishers 2013 Virus genes Vol.46 No.2
<P>Thirteen isolates of avian paramyxovirus type 4 (APMV-4) isolated from wild ducks in Korea from 2006 to 2011 were genetically characterized by sequence analysis of the N-terminal region of the APMV-4 fusion (F) protein gene. The results revealed that the amino acid sequence homology within Korean isolates was 97.5 % or greater. The homologies of the Korean isolates with the APMV-4/duck/HK/D3/75 and APMV-4/duck/BE/15129/07 strains were 86.9-88.0 and 95.5-96.1 %, respectively. All Korean isolates had sequence motifs of (116)DIQPRF(121) at the F0 cleavage site. Phylogenetic analysis based on the N-terminal region of the F protein gene of APMV-4 isolates revealed that all 2006-2011 Korean isolates formed a single genotypic cluster that was phylogenetically different from APMV-4/duck/HK/D3/75 or APMV-4/duck/BE/15129/07 strains. Korean APMV-4 isolates were more closely related to APMV-4/goose/ZA/N1468/10 (isolated in South Africa) than to the Belgium APMV-4 virus. Korean APMV-4 isolates were further divided into at least two subgroups (A and B) based on phylogenetic analysis. Subgroup A viruses were isolated throughout Korea, whereas subgroup B viruses were detected only in isolates from Cheju island in 2011, suggesting that Korean APMV-4 exhibits marked genetic diversity and differs from viruses currently circulating in Europe and other locations.</P>
Kang-Seuk Choi,Eun-Kyoung Lee,Woo-Jin Jeon,Jun-Hun Kwon 대한수의학회 2010 Journal of Veterinary Science Vol.11 No.3
Newcastle disease (ND) caused by virulent Newcastle disease virus (NDV) is a highly contagious viral disease of poultry. Virulent NDVs characteristically have a multibasic amino acid sequence (virulence motif) such as 112RRQKRF117 at the cleavage site of the precusor fusion (F0) protein. The antigenic and immunogenic characteristics of the virulence motif 112RRQKRF117 in the F0 protein of virulent NDVs were investigated. Epitope mapping analysis revealed that a RRQKRF-specific monoclonal antibody 4G2 recognized the KRF section of the motif. A synthetic peptide bearing the RRQKRF motif reacted strongly with sera from virulent NDV (with RRQKRF motif)-infected chickens. These sera also showed reactivity to peptides bearing other virulence motifs (112KRQKRF117, 112RRQRRF117 and 112RRRKRF117)but not an avirulence motif (112GRQGRL117) by ELISA. The synthetic bearing RRQKRF motif reacted with 60% to 91%of sera taken from surviving chickens on ND outbreak farms but not with sera from vaccinated birds, even though most of the sera had antibody to NDV due to vaccination. This indicates that the virulence motif has the potential to differentiate virulent NDV infected birds from vaccinated birds.
Choi, Kang-Seuk,Nah, Jin-Ju,Ko, Young-Joon,Kang, Shien-Young,Yoon, Kyoung-Jin,Jo, Nam-In American Society for Microbiology 2005 Clinical and diagnostic laboratory immunology Vol.12 No.1
<B>ABSTRACT</B><P>Attempts were made to identify and map epitopes on the nucleocapsid (N) protein of peste des petits ruminants virus (PPRV) (Nigeria75/1 strain) using seven monoclonal antibodies (MAbs) and deletion mutants. At least four antigenic domains (A-I, A-II, C-I, and C-II) were identified using the MAbs. Domains A-I (MAb 33-4) and A-II (MAbs 38-4, P-3H12, and P-13A9) were determined to be located on the amino-terminal half (amino acids [aa] 1 to 262), and domains C-I (P-14C6) and C-II (P-9H10 and P-11A6) were within the carboxy-terminal region (aa 448 to 521). Nonreciprocal competition between A-II MAbs and MAbs to C-I and C-II domains was observed, indicating that they may be exposed on the surface of the N protein and spatially overlap each other. Blocking or competitive enzyme-linked immunosorbent assay studies using PPRV serum antibodies revealed that epitopes on the domains A-II and C-II were immunodominant, whereas those on the domains A-I and C-I were not. The competition between MAb and rinderpest virus (RPV) serum antibodies raised against RPV strain LATC was found in two epitopes (P-3H12 and P-13A9) on the domain A-II, indicating that these epitopes may cause cross-reactivity between PPRV and RPV. Identification of immunodominant but PPRV-specific epitopes and domains will provide the foundation in designing an N-protein-based diagnostic immunoassay for PPRV.</P>
Choi, Kang-Seuk,Ko, Young-Joon,Nah, Jin-Ju,Kim, Yong-Joo,Kang, Shien-Young,Yoon, Kyoung-Jin,Joo, Yi-Seok American Society for Microbiology 2007 Clinical and vaccine immunology Vol.14 No.2
<B>ABSTRACT</B><P>A rapid immunoassay for detecting and quantifying West Nile virus (WNV)-neutralizing antibodies in sera was developed as an alternative to the plaque reduction neutralization test (PRNT), the gold standard test for WNV. The assay is a competitive, enzyme-linked immunosorbent assay using neutralizing monoclonal antibody 5E8 (NT-ELISA). A cutoff percent inhibition (PI) value of 35% (mean PI plus 3 standard deviations), with a specificity of 99%, was established based on analysis of 246 serum samples from horses free of WNV. The NT-ELISA detected neutralizing antibodies in all sera collected 7 or 14 days postinoculation from mice (<I>n</I> = 11) infected with lineage I (strain NY385-99) or II (strain B956) WNV. When sera from WNV-vaccinated horses (<I>n</I> = 212) were tested by NT-ELISA and PRNT, the NT-ELISA gave a positive result for 96.1% (173/180) of the PRNT-positive sera and 3.1% (1/32) of the PRNT-negative sera. Discrepancies between the two tests were observed mainly with sera with low PRNT90 titers (expressed as the reciprocal of the highest dilution yielding ≥90% reduction in the number of plaques) for WNV or low PIs by NT-ELISA. The overall agreement (<I>k</I> value) between the two tests was 0.86. A good correlation (<I>r</I><SUP>2</SUP> = 0.77) was also observed between the tests for endpoint titration of sera (<I>n</I> = 116). In conclusion, the newly developed NT-ELISA may be a good alternative serologic assay for detecting WNV that can be used for large-scale testing of WNV-neutralizing antibodies in multiple species.</P>
Kang-Seuk Choi,Eun-Kyoung Lee,Woo-Jin Jeon,Mi-Ja Park,Jin-Won Kim,Jun-Hun Kwon 대한수의학회 2009 JOURNAL OF VETERINARY SCIENCE Vol.10 No.4
Despite the existence of an active vaccination program, recently emerged strains of nephropathogenic infectious bronchitis virus (IBV) in Korea have caused significant economic losses in the poultry industry. In this study, we assessed the pathogenic and antigenic characteristics of a K-IIb type field strain of IBV that emerged in Korea since 2003, such as Kr/Q43/06. Specific pathogen free 1-weekold chickens exhibited severe respiratory symptoms (dyspnea) and nephropathogenic lesions (swollen kidneys with nephritis and urate deposits) following challenge with the recent IBV field strain. The antigenic relatedness (R value), based on a calculated virus neutralization index, of the K-IIb type field strain and K-IIa type strain KM91 (isolated in 1991) was 30%, which indicated that the recent strain, Kr/Q43/06, is a new variant that is antigenically distinct from strain KM91. This report is the first to document the emergence of a new antigenic variant of nephropathogenic IBV in chicken from Korea.