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Prof.
Georg Herrler has a long experience in the analysis of the
structure and function of the coronavirus surface proteins. His main focus
was directed on the initial stage of infection, the interaction of the
virus with cellular receptors. In his initial work his team demonstrated
that N-acetyl-9-O-acetylneuraminic acid serves as a receptor determinant on
cells susceptible to infection by bovine coronavirus and human coronavirus
OC43. Later work showed that porcine transmissible gastroenteritis virus
has a sialic acid binding activity that is essential for
enteropathogenicity. In addition to coronavirus glycoproteins, his research
team also analyses the glycoproteins of negative-stranded RNA viruses using
molecular biological techniques including reverse genetics. Applying a
combination of cell biology and molecular biology, he also made important
contributions concerning the surface transport of viral glycoproteins in
polarized epithelial cells. In more than 90 publications and reviews, Prof.
Herrler has proven his expertise in the research on viral glycoproteins.
Over the years, he coordinated numerous research projects with success.
Selected
publications of Partner 5:
- Zimmer G., Bossow S.,
Kolesnikova L., Hinz M., Neubert W.J. and Herrler, G. 2005. A chimeric
respiratory syncytial virus fusion protein functionally replaces the F
and HN glycoproteins in recombinant Sendai virus. J. Virol.
79:10467-1047.
- Hanika
A., Larisch B., Steinmann E., Schwegmann-Weßels C., Herrler G., and Zimmer G. 2005. Use of influenza C virus
glycoprotein HEF for generation of vesicular stomatitis virus
pseudotypes. J. Gen. Virol. 86:1455-1465.
- Schwegmann-Weßels C.,
Al-Falah M., Esocrs D., Wang Z., Zimmer G., Deng H., Enjuanes L., Naim
H., and Herrler G. 2004. A novel sorting signal for intracellular
localization is present in the S protein of a porcine coronavirus but
absent from severe acute respiratory syndrome-associated coronavirus.
J. Biol. Chem. 279:43661-43666.
- Köhl
W., Zimmer G., Greiser-Wilke I., Haas L., Moennig V., and Herrler G. 2004. The surface glycoprotein
E2 of bovine viral diarrhoea virus contains an intracellular
localization signal. J. Gen. Virol. 85:1101-1111.
- Zimmer G., McGregor G.
P., Rohn M., Schemann M., Conzelmann K.-K. and Herrler, G. 2003.
Virokinin, a bioactive peptide of the tachykinin family, is released
from the bovine respiratory syncytial virus fusion protein. J. Biol.
Chem. 278:46854-46861.
- Schwegmann-Wessels C.,
Zimmer G., Schröder B., Breves G., and Herrler G. 2003. Binding of
transmissible gastroenteritis coronavirus (TGEV) to brush border
membrane sialoglycoproteins. J.Virol. 77:11846-11848.
- Zimmer G., Zimmer K.P.,
Trotz I., and Herrler G. 2002.
Vesicular stomatitis virus glycoprotein does not determine the site of
virus release in polarized epithelial cells. J. Virol.
76:4103–4107.
- Schwegmann-Wessels C.,
Zimmer G., Laude H., Enjuanes L., and Herrler G. 2002. Binding of
transmissible gastroenteritis coronavirus to cell surface
sialoglycoproteins. J. Virol. 76:6037–6043.
- Zimmer G., Conzelmann
K.K., and Herrler G. 2002. Cleavage at the furin consensus sequence
RAR/KR(109) and presence of the intervening peptide of the respiratory
syncytial virus fusion protein are dispensable for virus replication
in cell culture. J. Virol. 76:9218–9224.
- Krempl C., and Herrler,
G. 2001. Sialic acid binding activity of transmissible gastroenteritis
corona-virus affects sedimentation behavior of virions and solubilized
glycoproteins. J. Virol. 75:844-849.
Prof. Georg Herrler
Georg.Herrler@tiho-hannover.de
Carolin Huettinger
Carolin.huettinger@tiho-hannover.de
Dr.
Christel Schwegmann-Weßels
Christel.Schwegmann@tiho-hannover.de
Jörg Glende
Joerg.Glende@tiho-hannover.de
Xiaofeng Ren
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