Molekulare Charakterisierung der Masernvirus-Ausbreitung aus polarisierten Epithelzellen

Applicant Professorin Dr. Andrea Susanne Maisner

Subject Area Virology

Term from 1999 to 2009

Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 5216804

Final Report Year 2008

Final Report Abstract

No abstract available

(2001). A single amino acid change in the cytoplasmic domains of measles virus glycoproteins H and F alters targeting, endocytosis and fusion in polarized Madin-Darby canine kidney cells. J. Biol. Chem. 276:17887-17894
Moll, M., Klenk, H.-D., Herrler, G., and A. Maisner
(2002). Importance of the cytoplasmic tails of the measles virus glycoproteins for fusogenic activity and the generation of recombinant measles viruses. J. Virol. 76:7174-7186
Moll, M., Klenk, H.-D., and A. Maisner
(2002). Measles virus matrix protein is not cotransported with the viral glycoproteins but requires virus infection for efficient surface targeting. Virus Res. 83:1-12
Riedl, P., Moll, M., Klenk, H.-D., and A. Maisner
(2004). Polarized glycoprotein targeting affects spread of measles virus in vitro and in vivo. J. Gen. Virol. 85:1019-1027
Moll, M., Pfeuffer, J., Klenk, H.-D., Niewiesk, S., and A. Maisner
(2007). Measles virus nucieocapsid transport to the plasma membrane requires stable expression and surface accumulation of the viral matrix protein. Cell. Microbiol. 9:1203-1214
Runkler, N., Pohl, C., Schneider-Schaulies, S., Klenk, H.-D., and A. Maisner
(2008). Glycoprotein targeting signals influence the distribution of measles virus envelope proteins and virus spread in lymphocytes. J. Gen. Virol. 89: 687-696
Runkler, N., Moll, M., Klenk, H.-D., and A. Maisner