Association of respiratory syncytial virus M protein with viral nucleocapsids is mediated by the M2-1 protein.

Cytoplasmic inclusions in respiratory syncytial virus-infected cells comprising viral nucleocapsid proteins (L, N, P, and M2-1) and the viral genome are sites of viral transcription. Although not believed to be necessary for transcription, the matrix (M) protein is also present in these inclusions, and we have previously shown that M inhibits viral transcription. In this study, we have investigated the mechanisms for the association of the M protein with cytoplasmic inclusions.

Inhibition of airway Na+ transport by respiratory syncytial virus.

In previous studies, we have shown that two major respiratory pathogens, influenza virus and parainfluenza virus, produce acute alterations in ion transport upon contacting the apical membrane of the respiratory epithelium. In the present study, we examine the effects on ion transport by the mouse tracheal epithelium of a third major respiratory pathogen, respiratory syncytial virus (RSV). RSV infections are associated with fluid accumulation in the respiratory tract and cause illnesses that range in severity from rhinitis, sinusitis, otitis media, and bronchitis to bronchiolitis and pneumonia.

Type 1 and 2 immunity following vaccination is influenced by nanoparticle size: formulation of a model vaccine for respiratory syncytial virus.

Previous studies compared uptake by dendritic cells (DC) of 20, 40, 100, 200, 500, 1000, and 2000 nm beads in vivo. When beads were used as antigen carriers, bead size influenced antibody responses and induction of IFN-gamma-producing CD4 and CD8 T cells. Beads of 40-50 nm were taken up preferentially by DC and induced particularly strong immunity.

Interaction between the respiratory syncytial virus G glycoprotein cytoplasmic domain and the matrix protein.

Paramyxovirus assembly at the cell membrane requires the movement of viral components to budding sites and envelopment of nucleocapsids by cellular membranes containing viral glycoproteins, facilitated by interactions with the matrix protein. The specific protein interactions during assembly of respiratory syncytial virus (RSV) are unknown. Here, the postulated interaction between the RSV matrix protein (M) and G glycoprotein (G) was investigated.

The viral manipulation of the host cellular and immune environments to enhance propagation and survival: a focus on RNA viruses.

Virus infection presents a significant challenge to host survival. The capacity of the virus to replicate and persist in the host is dependent on the status of the host antiviral defense mechanisms. The study of antiviral immunity has revealed effective antiviral host immune responses and enhanced our knowledge of the diversity of viral immunomodulatory strategies that undermine these defences.

Detection and subgrouping of respiratory syncytial virus directly from nasopharyngeal aspirates.

OBJECTIVE: To develop a reverse transcription-polymerase chain reaction (RT-PCR)-based assay to identify the subgroup of the infecting respiratory syncytial virus (RSV) strain directly from nasopharyngeal aspirates (NPAs). METHODS: A total of 154 NPAs which were positive for RSV antigen by direct immunofluorescence were subjected to RT-PCR. The primers used were designed to give products for subgroup A and B which were of different sizes and easily visualized on agarose electrophoresis.