Hemagglutinin Neuraminidase Hn Gene
Mostrando 1-12 de 29 artigos, teses e dissertações.
-
1. RT-PCR for detection on bovine parainfluenza virus type 3 (bPIV-3) = RT-PCR para detecção do vírus parainfluenza bovino tipo 3 (bPIV-3) / RT-PCR para detecção do vírus parainfluenza bovino tipo 3 (bPIV-3)
A técnica de RT-PCR tem sido freqüentemente utilizada para a detecção do vírus parainfluenza humano tipo 3 (hPIV- 3), mas a literatura é escassa em relação ao vírus parainfluenza bovino tipo 3 (bPIV-3) .O objetivo deste trabalho foi descrever uma técnica de reação em cadeia pela polimerase, precedida de transcrição reversa (RT-PCR), para a dete
Publicado em: 2010
-
2. Structure-function analysis of two variants of mumps virus hemagglutinin-neuraminidase protein
A point mutation from guanine (G) to adenine (A) at nucleotide position 1081 in the hemagglutinin-neuraminidase (HN) gene has been associated with neurovirulence of Urabe AM9 mumps virus vaccine. This mutation corresponds to a glutamic acid (E) to lysine (K) change at position 335 in the HN glycoprotein. We have experimentally demonstrated that two variants
Brazilian Journal of Infectious Diseases. Publicado em: 2009-02
-
3. Desenvolvimento de técnicas de RT-PCR para seqënciamento do gene da hemaglutinina-neuraminidase (HN) e detecção do vírus Parainfluenza bovino tipo 3 / Development of RT-PCR techniques for hemagglutinin-neuraminidase (HN) gene sequencing and detection of bovine type 3 Parainfluenza virus
Existem diversos trabalhos publicados sobre a utilização de diferentes métodos imunológicos para diagnosticar infecções do trato respiratório causadas por vírus parainfluenza bovino tipo 3 (bPIV-3). Entretanto, é escassa a literatura sobre a utilização da técnica de isolamento viral. Até o presente momento não havia sido relatada a utilização
Publicado em: 2007
-
4. Antigenic and structural properties of the hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3: sequence analysis of variants selected with monoclonal antibodies which inhibit infectivity, hemagglutination, and neuraminidase activities.
The hemagglutinin-neuraminidase (HN) gene sequence was determined for 16 antigenic variants of human parainfluenza virus type 3 (PIV3). The variants were selected by using monoclonal antibodies (MAbs) to the HN protein which inhibit neuraminidase, hemagglutination, or both activities. Each variant had a single-point mutation in the HN gene, coding for a sing
-
5. Mutations in Human Parainfluenza Virus Type 3 Hemagglutinin-Neuraminidase Causing Increased Receptor Binding Activity and Resistance to the Transition State Sialic Acid Analog 4-GU-DANA (Zanamivir)
Entry and fusion of human parainfluenza virus type 3 (HPF3) require the interaction of the viral hemagglutinin-neuraminidase (HN) glycoprotein with its sialic acid receptor. 4-GU-DANA, a potent inhibitor of influenza virus neuraminidase, inhibits not only HPF3 neuraminidase but also the receptor binding activity of HPF3 HN and thus its ability to promote att
American Society for Microbiology.
-
6. The Hemagglutinin-Neuraminidase Protein of Newcastle Disease Virus Determines Tropism and Virulence
The hemagglutinin-neuraminidase (HN) protein of Newcastle disease virus (NDV) plays a crucial role in the process of infection. However, the exact contribution of the HN gene to NDV pathogenesis is not known. In this study, the role of the HN gene in NDV virulence was examined. By use of reverse genetics procedures, the HN genes of a virulent recombinant NDV
American Society for Microbiology.
-
7. A Single Amino Acid Alteration in the Human Parainfluenza Virus Type 3 Hemagglutinin-Neuraminidase Glycoprotein Confers Resistance to the Inhibitory Effects of Zanamivir on Receptor Binding and Neuraminidase Activity
Entry and fusion of human parainfluenza virus type 3 (HPF3) requires interaction of the viral hemagglutinin-neuraminidase (HN) glycoprotein with its sialic acid receptor. 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid (4-GU-DANA; zanamivir), a sialic acid transition-state analog designed to fit the influenza virus neuraminidase catalytic site, p
American Society for Microbiology.
-
8. Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses.
The fusion glycoprotein (F) and hemagglutinin-neuraminidase (HN) genes of human parainfluenza virus type 2 (PI2) were molecularly cloned and expressed in HeLa-T4 cells by using the vaccinia virus-T7 transient expression system. Expression of the F and HN proteins was detected by using immunoprecipitation and surface immunofluorescence staining. Although the
-
9. Efficacy of Novel Hemagglutinin-Neuraminidase Inhibitors BCX 2798 and BCX 2855 against Human Parainfluenza Viruses In Vitro and In Vivo
Human parainfluenza viruses are important respiratory tract pathogens, especially of children. However, no vaccines or specific therapies for infections caused by these viruses are currently available. In the present study we characterized the efficacy of the novel parainfluenza virus inhibitors BCX 2798 and BCX 2855, which were designed based on the three-d
American Society for Microbiology.
-
10. The Novel Parainfluenza Virus Hemagglutinin-Neuraminidase Inhibitor BCX 2798 Prevents Lethal Synergism between a Paramyxovirus and Streptococcus pneumoniae
An association exists between respiratory viruses and bacterial infections. Prevention or treatment of the preceding viral infection is a logical goal for reducing this important cause of morbidity and mortality. The ability of the novel, selective parainfluenza virus hemagglutinin-neuraminidase inhibitor BCX 2798 to prevent the synergism between a paramyxov
American Society for Microbiology.
-
11. Human Parainfluenza Virus Type 3 HN-Receptor Interaction: Effect of 4-Guanidino-Neu5Ac2en on a Neuraminidase-Deficient Variant
The envelope of human parainfluenza virus type 3 (HPF3) contains two viral glycoproteins, the hemagglutinin-neuraminidase (HN) and the fusion protein (F). HN, which is responsible for receptor attachment and for promoting F-mediated fusion, also possesses neuraminidase (receptor-destroying) activity. We reported previously that 4-guanidino-neu5Ac2en (4-GU-DA
American Society for Microbiology.
-
12. Interacting Domains of the HN and F Proteins of Newcastle Disease Virus
The activation of most paramyxovirus fusion proteins (F proteins) requires not only cleavage of F0 to F1 and F2 but also coexpression of the homologous attachment protein, hemagglutinin-neuraminidase (HN) or hemagglutinin (H). The type specificity requirement for HN or H protein coexpression strongly suggests that an interaction between HN and F proteins is
American Society for Microbiology.