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Adolescent , Humans , Male , Female , Smoking Cessation , Smoking , Smoking PreventionABSTRACT
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Humans , Male , Female , Essential Hypertension , Obesity , Waist Circumference , Body Mass Index , Cardiovascular DiseasesABSTRACT
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Hospital Costs , Hospitals , Length of Stay , Hospitals, High-Volume , Cost of Illness , Insurance, Health , Surgical Procedures, OperativeABSTRACT
Haemorrhagic fever with renal syndrome (HFRS) caused by Hantaan viruses has been one of the principal acute febrile disease in Korea. To analysis the sero-epidemiological patterns of HFRS, 4,177 patient sera of acute febrile illness submitted for serological assay to National Institute of Health from Community Health Centers, Institutes of Health and Environment and hospitals from 1996 to 2005 were examined for antibodies against Hantaan virus by indirect immunofluorescent assay (IFA). Serum samples with greater than 1:32 antibody titer were considered positive. The results were analyzed seroepidemiologically by annual, sexual, seasonal, age and regional distribution of HFRS patients. Out of 4,177 serum samples tested, 1,415 samples (33.9%) were positive to Hantaan virus. The ratio of males (48.2%, 682/1,415) to females (38.2%, 541/1,415) was 1.3:1. Seasonal incidence showed that 69.5% (985/1,415) of cases occurred from October to December, resulting with higher prevalence in November (41.3%, 584/1,415). Regionally, seropositive rates of samples collected in Gyenggi, Gangwon and Chungbuk were 39.9% (564/1,415), 19.3% (274/1,415) and 8.5% (120/1,1415), respectively. Age distributions of seropositive of HFRS were detected from 20 to 79 years (78%).
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Female , Humans , Male , Academies and Institutes , Age Distribution , Antibodies , Community Health Centers , Fever , Hantaan virus , Hemorrhagic Fever with Renal Syndrome , Incidence , Korea , Prevalence , SeasonsABSTRACT
To investigate the pattern of drug-resistance of human influenza virus (A/H1N1) isolated in Korea during 2001~2002, the sequence analysis of hemagglutinin (HA) and neuraminidase (NA) genes and cell-based assay against neuraminidase inhibitor (NI) were performed. Analyses on the nucleotide sequences of NA genes showed that Korean isolates had 98.2 to 98.5% homology with that of the vaccine strain in 2001~2002 season, A/New Caledonia/20/99-like strain. However, there were no significant amino acid substitutions related to the drug-resistance such as E119V, R152K, I222R/Q, H274Y, and R292K. In the sequences of HA gene, no differences were observed on the major antigenic sites as well as the motifs related to the drug resistance. 50% inhibitory concentration (IC50) value against oseltamivir, one of NA inhibitors widely used in the treatment for the influenza, was determined by WST-1 assay. The SI values of Korean isolates against oseltamivir were 7.2 to 383.3, showing that these isolates displayed relatively low SI value against the drug. This result provides the useful information for the surveillance of drug-resistant influenza virus and the control of influenza in Korea.
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Amino Acid Substitution , Base Sequence , Drug Resistance , Hemagglutinins , Influenza, Human , Korea , Neuraminidase , Orthomyxoviridae , Oseltamivir , Seasons , Sequence AnalysisABSTRACT
Japanese encephalitis is a potentially lethal disease of the central nervous system caused by infection with Japanese encephalitis virus (JEV). JEV is the most common cause of encephalitis over a large part of eastern Asia. To establish and characterize in vivo model to study the Japanese encephalitis, the immunohistochemical localization of JEV and the histopathological finding were investigated in the brains of young adult mice infected with JEV by intraperitoneal inoculation. JEV was localized to neurons in discrete regions of the brain. Histopathological finding showed typical pattern of acute viral encephalitis, such as inflammatory cell infiltration in brain parenchyme and perivascular cuffs of mononuclear cells. These results suggest that this in vivo system can be used to study the mechanism of virus entry into the brain, cell specific tropism, and pathophysiology in Japanese encephalitis.
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Animals , Humans , Mice , Young Adult , Asian People , Brain , Central Nervous System , Encephalitis , Encephalitis Virus, Japanese , Encephalitis, Japanese , Encephalitis, Viral , Asia, Eastern , Immunohistochemistry , Neurons , Tropism , Virus InternalizationABSTRACT
Envelope glycoprotein 1 (G1) and glycoprotein 2 (G2) of Hantaan (HTN) virus are believed to be major viral antigens that can induce neutralizing immunity against HTN virus infection. The purpose of this study is to clone and express G1 gene in an E. coli expression system. The truncated G1 gene (amino acid residues 35 to 123) of the HTN virus strain 76-118 was amplified by polymerase chain reaction (PCR). The 0.28 kb PCR product was cloned into pCR2.1 vector and named as pCGS1. The truncated G1 gene was excised from the pCGS1 and subcloned into the BamHI and SalI sites of pGEX-4T-2 and named pGGS1. The nucleotide sequence of the 0.28 kb truncated G1 gene was determined. It is revealed four non-silent nucleotide substitutions between the published sequence of strain HTN virus strain 76-118 and our stock of HTN virus strain 76-118 (passaged several times in our laboratory). The first G1 mutation was found to constitute an A to G nucleotide substitution, giving raise to an asparagine to serine mutation at residue 64. The second G1 mutation was found to constitute an A to C nucleotide substitution, giving raise to an lysine to threonine mutation at residue 112. The third G1 mutation was found to constitute an A to C nucleotide substitution, giving raise to an lysine to threonine mutation at residue 112. The fourth G1 mutation was found to constitute an G to A nucleotide substitution, giving raise to an glutamic acid to lysine mutation at residue 117. The truncated G1 gene was expressed as a 37 kDa protein fused to glutathione-S-transferase (GST). The GST fusion protein was purified by Glutathione Sepharose 4B affinity chromatography and reacted with the sera from patients of hemorrhage fever with renal syndrome (HFRS). One of 12 serum samples from HFRS patients was reactive with the 37 kDa fusion protein strongly. Three sera reacted moderately with the fusion protein. Six sera reacted only weakly with the protein, while remaing two were non-reactive. Control sera from patients with scrub typhus leptospirosis, or negative HFRS did not react with the recombinant fusion protein.