부산대학교 도서관

Mumps virus (MuV) is the etiological agent of mumps, a disease characterized by painful swelling of the parotid glands and often accompanied by severe complications. To understand the molecular mechanism of MuV infection, a functional analysis of the involved host factors is required. However, little is known about the host factors involved in MuV infection, especially those involved in the late stage of infection. Here, we identified 638 host proteins that have close proximity to MuV glycoproteins, which are a major component of the viral particles, by proximity labeling and examined comprehensive protein–protein interaction networks of the host proteins. From siRNA screening and immunoprecipitation results, we found that a SNARE subfamily protein, USE1, bound specifically to the MuV fusion (F) protein and was important for MuV propagation. In addition, USE1 plays a role in complete N-linked glycosylation and expression of the MuV F protein. Author summary: The family Paramyxoviridae includes several important human and animal pathogens such as mumps virus (MuV), which is the etiological agent of mumps. Viral particle formation, the final stage of viral infection, is a complex and integrated step in which all of the particle components accumulate and assemble. To understand the molecular mechanism of this stage of MuV infection, we searched for host proteins that came into close proximity to the cytoplasmic domain of viral membrane proteins, which are a major viral particle component. We generated comprehensive protein–protein interaction networks of the obtained host proteins and found that a SNARE subfamily protein, USE1, was important for the efficient MuV propagation. Furthermore, this protein bound specifically to the MuV F protein and was important for the functional maturation of F protein through complete N-linked glycosylation and expression. [ABSTRACT FROM AUTHOR]