Theoretically, in the tourism context this study introduced a new concept of non-pharmaceutical intervention (NPI) for influenza, and tested the impact of NPI on the behavioral intention of potential international tourists. This study also extended the model of goal-directed behavior (MGB) by incorporating the new concepts of NPI, and the perception of 2009 H1N1.
The model found that desire, perceived behavioral control, frequency of past behavior, and non-pharmaceutical interventions predicted tourists’ intention but perceptions of 2009 H1N1 had nil effect on desire and intention. Personal non-pharmaceutical interventions were theorized as adaptive behavior of tourists intending to travel during a pandemic which should be supported by tourism operators on a system-wide basis.
Description: Goat polyclonal antibody to tdTomato (red fluorescent protein). tdTomato protein is derived from DsRed, an engineered red fluorescent protein from so-called disc corals of the genus Discosoma. It is a genetic fusion of two copies of the dTomato gene, which has been specifically designed for low aggregation. It´s brightness and emission wavelength makes it ideal for live animal research.
Description: Goat polyclonal antibody to tdTomato (red fluorescent protein). tdTomato protein is derived from DsRed, an engineered red fluorescent protein from so-called disc corals of the genus Discosoma. It is a genetic fusion of two copies of the dTomato gene, which has been specifically designed for low aggregation. It is a ~54 kDa protein that is optimally excited at a 554 nm and has a maximum of emission at 581 nm. It´s brightness and emission wavelength, makes it ideal for live animal research.
Description: Goat polyclonal antibody to tdTomato (red fluorescent protein) conjugated to DyLight® 405. tdTomato protein is derived from DsRed, an engineered red fluorescent protein from so-called disc corals of the genus Discosoma. It is a genetic fusion of two copies of the dTomato gene, which has been specifically designed for low aggregation. It´s brightness and emission wavelength, makes it ideal for live animal research.
Description: Goat polyclonal antibody to tdTomato (red fluorescent protein) conjugated to DyLight® 488. tdTomato protein is derived from DsRed, an engineered red fluorescent protein from so-called disc corals of the genus Discosoma. It is a genetic fusion of two copies of the dTomato gene, which has been specifically designed for low aggregation. It´s brightness and emission wavelength, makes it ideal for live animal research.
Description: Goat polyclonal antibody to tdTomato (red fluorescent protein) conjugated to DyLight® 550. tdTomato protein is derived from DsRed, an engineered red fluorescent protein from so-called disc corals of the genus Discosoma. It is a genetic fusion of two copies of the dTomato gene, which has been specifically designed for low aggregation. It´s brightness and emission wavelength, makes it ideal for live animal research.
Description: Goat polyclonal antibody to tdTomato (red fluorescent protein) conjugated to DyLight® 633. tdTomato protein is derived from DsRed, an engineered red fluorescent protein from so-called disc corals of the genus Discosoma. It is a genetic fusion of two copies of the dTomato gene, which has been specifically designed for low aggregation. It´s brightness and emission wavelength, makes it ideal for live animal research.
Description: This gene is a member of the DNA polymerase type-X family and encodes a template-independent DNA polymerase that catalyzes the addition of deoxynucleotides to the 3'-hydroxyl terminus of oligonucleotide primers. In vivo, the encoded protein is expressed in a restricted population of normal and malignant pre-B and pre-T lymphocytes during early differentiation, where it generates antigen receptor diversity by synthesizing non-germ line elements (N-regions) at the junctions of rearranged Ig heavy chain and T cell receptor gene segments. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.
Description: This gene is a member of the DNA polymerase type-X family and encodes a template-independent DNA polymerase that catalyzes the addition of deoxynucleotides to the 3'-hydroxyl terminus of oligonucleotide primers. In vivo, the encoded protein is expressed in a restricted population of normal and malignant pre-B and pre-T lymphocytes during early differentiation, where it generates antigen receptor diversity by synthesizing non-germ line elements (N-regions) at the junctions of rearranged Ig heavy chain and T cell receptor gene segments. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.
Description: Terminal Deoxynucleotidyl Transferase, also known as Terminal transferase, is a unique DNA polymerase that without template direction catalyzes the addition of deoxyribonucleotides onto the 3-prime-hydroxyl end of DNA primers. Its gene is mapped to the region 10q23-q24. And TdT cDNA contains an open reading frame of 1,530 basepairs corresponding to a protein containing 510 amino acids. TdT may be responsible for inserting nucleotides (N regions) at the V(H)-D and D-J(H) junctions of immunoglobulin genes. The enzyme is present in immature thymocytes, some bone marrow cells, transformed pre-B and pre-T cell lines, and leukemia cells. Additionally, TdT catalyses the addition of nucleotides to the 3' terminus of a DNA molecule. Unlike most DNA polymerases it does not require a template. The preferred substrate of this enzyme is a 3'-overhang, but it can also add nucleotides to blunt or recessed 3' ends. Cobalt is a necessary cofactor.
Description: Terminal deoxynucleotidyltransferase is a template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. [UniProt]
Description: Terminal deoxynucleotidyltransferase (TdT) is a DNA polymerase which catalyzes the addition of deoxyribonucleotides onto the 3 termini of DNA. The human TdT gene maps to chromosome 10q24.1 and encodes a 510 amino acid protein. Human TdT is synthesized as a single chain peptide that elicits a minor preference for incorporation of deoxyribonucleotides over ribonucleotides forming DNA strands. It is present in immature thymocytes, some bone marrow cells, transformed pre-B and pre-T cell lines, and leukemia cells.
Description: Terminal deoxynucleotidyltransferase (TdT) is a DNA polymerase which catalyzes the addition of deoxyribonucleotides onto the 3 termini of DNA. The human TdT gene maps to chromosome 10q24.1 and encodes a 510 amino acid protein. Human TdT is synthesized as a single chain peptide that elicits a minor preference for incorporation of deoxyribonucleotides over ribonucleotides forming DNA strands. It is present in immature thymocytes, some bone marrow cells, transformed pre-B and pre-T cell lines, and leukemia cells.
Description: Terminal deoxynucleotidyltransferase (TdT) is a DNA polymerase which catalyzes the addition of deoxyribonucleotides onto the 3 termini of DNA. The human TdT gene maps to chromosome 10q24.1 and encodes a 510 amino acid protein. Human TdT is synthesized as a single chain peptide that elicits a minor preference for incorporation of deoxyribonucleotides over ribonucleotides forming DNA strands. It is present in immature thymocytes, some bone marrow cells, transformed pre-B and pre-T cell lines, and leukemia cells.
Description: Terminal deoxynucleotidyltransferase (TdT) is a DNA polymerase which catalyzes the addition of deoxyribonucleotides onto the 3 termini of DNA. The human TdT gene maps to chromosome 10q24.1 and encodes a 510 amino acid protein. Human TdT is synthesized as a single chain peptide that elicits a minor preference for incorporation of deoxyribonucleotides over ribonucleotides forming DNA strands. TdT is present in immature thymocytes, some bone marrow cells, transformed pre-B and pre-T cell lines, and leukemia cells.
Description: Terminal deoxynucleotidyltransferase (TdT) is a DNA polymerase which catalyzes the addition of deoxyribonucleotides onto the 3 termini of DNA. The human TdT gene maps to chromosome 10q24.1 and encodes a 510 amino acid protein. Human TdT is synthesized as a single chain peptide that elicits a minor preference for incorporation of deoxyribonucleotides over ribonucleotides forming DNA strands. TdT is present in immature thymocytes, some bone marrow cells, transformed pre-B and pre-T cell lines, and leukemia cells.
Description: Terminal deoxynucleotidyltransferase (TdT) is a DNA polymerase which catalyzes the addition of deoxyribonucleotides onto the 3 termini of DNA. The human TdT gene maps to chromosome 10q24.1 and encodes a 510 amino acid protein. Human TdT is synthesized as a single chain peptide that elicits a minor preference for incorporation of deoxyribonucleotides over ribonucleotides forming DNA strands. TdT is present in immature thymocytes, some bone marrow cells, transformed pre-B and pre-T cell lines, and leukemia cells.
Description: This gene is a member of the septin gene family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is mapped to 22q11, the region frequently deleted in DiGeorge and velocardiofacial syndromes. A translocation involving the MLL gene and this gene has also been reported in patients with acute myeloid leukemia. Alternative splicing results in multiple transcript variants. The presence of a non-consensus polyA signal (AACAAT) in this gene also results in read-through transcription into the downstream neighboring gene (GP1BB; platelet glycoprotein Ib), whereby larger, non-coding transcripts are produced.
Description: This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Description: This gene is a member of the septin gene family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is mapped to 22q11, the region frequently deleted in DiGeorge and velocardiofacial syndromes. A translocation involving the MLL gene and this gene has also been reported in patients with acute myeloid leukemia. Alternative splicing results in multiple transcript variants. The presence of a non-consensus polyA signal (AACAAT) in this gene also results in read-through transcription into the downstream neighboring gene (GP1BB; platelet glycoprotein Ib), whereby larger, non-coding transcripts are produced.
Description: This gene is a member of the septin family of GTPases. Members of this family are required for cytokinesis. One version of pediatric acute myeloid leukemia is the result of a reciprocal translocation between chromosomes 11 and X, with the breakpoint associated with the genes encoding the mixed-lineage leukemia and septin 2 proteins. This gene encodes four transcript variants encoding three distinct isoforms. An additional transcript variant has been identified, but its biological validity has not been determined.
Description: This gene is a member of the septin family involved in cytokinesis and cell cycle control. This gene is a candidate for the ovarian tumor suppressor gene. Mutations in this gene cause hereditary neuralgic amyotrophy, also known as neuritis with brachial predilection. A chromosomal translocation involving this gene on chromosome 17 and the MLL gene on chromosome 11 results in acute myelomonocytic leukemia. Multiple alternatively spliced transcript variants encoding different isoforms have been described.
Description: This gene encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae. The protein also shares similarity with Diff 6 of Drosophila and with H5 of mouse. Each of these similar proteins, including the yeast CDC10, contains a GTP-binding motif. The yeast CDC10 protein is a structural component of the 10 nm filament which lies inside the cytoplasmic membrane and is essential for cytokinesis. This human protein functions in gliomagenesis and in the suppression of glioma cell growth, and it is required for the association of centromere-associated protein E with the kinetochore. Alternative splicing results in multiple transcript variants. Several related pseudogenes have been identified on chromosomes 5, 7, 9, 10, 11, 14, 17 and 19.
Description: This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is highly expressed in brain and heart. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. One of the isoforms (known as ARTS) is distinct; it is localized to the mitochondria, and has a role in apoptosis and cancer.
Description: This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Practically, this study dealt with the issue of influenza 2009 H1N1 with the study findings and implications providing government agencies, tourism marketers, policy-makers, transport systems, and hospitality services with important suggestions for NPI and international tourism during pandemics.
The impact of non-pharmaceutical interventions for 2009 H1N1 influenza on travel intentions: A model of goal-directed behavior.
Antiviral Activity of Fritillaria thunbergii extract against Human Influenza Virus H1N1 (PR8) in vitro, in ovo and in vivo.
.Influenza viruses cause respiratory diseases in humans and animals with high morbidity and mortality rates. Conventional anti-influenza drugs are reported to exert side-effects and newly emerging viral strains tend to develop resistance to these commonly used agents. Fritillaria thunbergii (FT) is traditionally used as an expectorant for controlling airway inflammatory disorders.
Here, we evaluated the therapeutic effects of FT extracts against influenza virus type A (H1N1) infection in vitro, in ovo, and in vivo. In the post-treatment assay, FT extracts showed high CC50 (7500 µg/ml) indicating low toxicity and exerted moderate antiviral effects, compared to Oseltamivir (SI 50.6 vs. 222) in vitro. Antiviral activity tests in ovo revealed strong inhibitory effects of both FT extract and Oseltamivir against H1N1 replication in embryonated eggs.
Notably, at a treatment concentration of 150 mg/kg, only half the group administered Oseltamivir survived whereas the FT group showed 100% survival, clearly supporting low toxicity of FT extracts. Consistent with these findings, FT-administered mice showed a higher survival rate with lower body weight reduction relative to the Oseltamivir group upon treatment 24 h after viral infection.
Our collective results suggest that FT extracts exert antiviral effects against influenza H1N1 virus without inducing toxicity in vitro, in ovo and in vivo, supporting its potential utility as a novel candidate therapeutic drug or supplement against influenza.
MicroRNA-132-3p suppress type I IFN response through targeting IRF1 to facilitate H1N1 influenza A virus infection.
Increasing evidence has indicated that microRNAs (miRNAs) have essential roles in innate immune responses to various viral infections; however, the role of miRNAs in H1N1 influenza A virus (IAV) infection is still unclear. The present study aimed to elucidate the role and mechanism of miRNAs in IAV replication in vitro. Using a microarray assay, we analyzed the expression profiles of miRNAs in peripheral blood from IAV patients. It was found that miR-132-3p was significantly upregulated in peripheral blood samples from IAV patients. It was also observed that IAV infection upregulated the expression of miR-132-3p in a dose and time dependent manner. Subsequently, we investigated miR-132-3p function and found that upregulation of miR-132-3p promoted IAV replication, whereas knockdown of miR-132-3p repressed replication.
Meanwhile, overexpression of miR-132-3p could inhibit IAV triggered INF-α and INF-β production and IFN-stimulated gene (ISG) expression , including myxovirus protein A (MxA), 2´, 5´-oligoadenylate synthetases (OAS), and double stranded RNA-dependent protein kinase (PKR), while inhibition of miR-132-3p enhanced IAV triggered these effects. Of note, interferon regulatory factor 1 (IRF1), a well-known regulator of the type I IFN response, was identified as a direct target of miR-132-3p during HIN1 IAV infection.
Furthermore, knockdown of IRF1 by si-IRF1 reversed the promoting effects of miR-132-3p inhibition on type I IFN response. Taken together, upregulation of miR-132-3p promotes IAV replication by suppressing type I IFN response through its target gene IRF1, suggesting that miR-132-3p could represent a novel potential therapeutic target of IAV treatment.
