Polarized Budding of Measles Virus Is Not Determined by Viral Surface Glycoproteins
AUTOR(ES)
Maisner, A.
FONTE
American Society for Microbiology
RESUMO
For viruses that mature by a budding process, the envelope glycoproteins are considered the major determinants for the site of virus release from polarized epithelial cells. Viruses are usually released from that membrane domain where the viral surface glycoproteins are transported to. We here report that measles virus has developed a different maturation strategy. Measles virus was found to be released from the apical membrane domain of polarized epithelial cells, though the surface glycoproteins H and F were transported in a nonpolarized fashion and to the basolateral membrane domain, respectively.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=110120Documentos Relacionados
- Measles Virus-Induced Immunosuppression In Vitro Is Independent of Complex Glycosylation of Viral Glycoproteins and of Hemifusion
- CD150 (SLAM) Is a Receptor for Measles Virus but Is Not Involved in Viral Contact-Mediated Proliferation Inhibition
- Interaction of measles virus glycoproteins with the surface of uninfected peripheral blood lymphocytes induces immunosuppression in vitro
- Cell fusion induced by herpes simplex virus is promoted and suppressed by different viral glycoproteins.
- Kinetics of protective antibodies are determined by the viral surface antigen