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Receptor Recognition by a Hepatitis B Virus Reveals a Novel Mode of High Affinity Virus-Receptor Interaction

Title data

Urban, Stephan ; Schwarz, Caroline ; Marx, Ute C. ; Zentgraf, Hanswalter ; Schaller, Heinz ; Multhaup, Gerd:
Receptor Recognition by a Hepatitis B Virus Reveals a Novel Mode of High Affinity Virus-Receptor Interaction.
In: The EMBO Journal. Vol. 19 (March 2000) Issue 6 . - pp. 1217-1227.
ISSN 0261-4189
DOI: https://doi.org/10.1093/emboj/19.6.1217

Abstract in another language

The duck hepatitis B virus model system was used to elucidate the characteristics of receptor (carboxypeptidase D, gp180) interaction with polypeptides representing the receptor binding site in the preS part of the large viral surface protein. We demonstrate the pivotal role of carboxypeptidase D for virus entry and show its C-domain represents the virus attachment site, which binds preS with extraordinary affinity. Combining results from surface plasmon resonance spectroscopy and two-dimensional NMR analysis we resolved the contribution of preS sequence elements to complex stability and show that receptor binding potentially occurs in two steps. Initially, a short α–helix in the C–terminus of the receptor binding domain facilitates formation of a primary complex. This complex is stabilized sequentially, involving ∼60 most randomly structured amino acids preceding the helix. Thus, hepadnaviruses exhibit a novel mechanism of high affinity receptor interaction by conserving the potential to adapt structure during binding rather than to preserve it per se. We propose that this process represents an alternative strategy to escape immune surveillance and the evolutionary pressure inherent in the compact hepadnaviral genome organization.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Chair Biopolymers - Univ.-Prof. Dr. Paul Rösch
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 24 Jan 2019 09:59
Last Modified: 16 May 2019 05:37
URI: https://eref.uni-bayreuth.de/id/eprint/47018