Dimerization of matrix protein is required for budding of respiratory syncytial virus.

ABSTRACT:

Unlabelled

Respiratory syncytial virus (RSV) infects epithelial cells of the respiratory tract and is a major cause of bronchiolitis and pneumonia in children and the elderly. The virus assembles and buds through the plasma membrane, forming elongated membrane filaments, but details of how this happens remain obscure. Oligomerization of the matrix protein (M) is a key step in the process of assembly and infectious virus production. In addition, it was suggested to affect the conformation of the fusion protein, the major current target for RSV antivirals, in the mature virus. The structure and assembly of M are thus key parameters in the RSV antiviral development strategy. The structure of RSV M was previously published as a monomer. Other paramyxovirus M proteins have been shown to

SUBMITTER: Forster A 

PROVIDER: S-EPMC4442381 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature