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Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules

Title data

Scholz, Christian ; Schaarschmidt, Peter ; Engel, Alfred M. ; Andres, Herbert ; Schmitt, Urban ; Faatz, Elke ; Balbach, Jochen ; Schmid, Franz X.:
Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules.
In: Journal of Molecular Biology. Vol. 345 (4 February 2005) Issue 5 . - pp. 1229-1241.
ISSN 0022-2836
DOI: https://doi.org/10.1016/j.jmb.2004.10.091

Abstract in another language

The envelope proteins of human immunodeficiency virus (HIV) and human T-cell lymphotrophic virus (HTLV) mediate cell attachment and membrane fusion. For HIV-1, the precursor protein gp160 is cleaved proteolytically into two fragments, the surface-associated receptor binding subunit gp120 and the membrane spanning subunit gp41, which is involved in membrane fusion during virus entry. Soluble and immunoreactive variants of gp41 are essential for the reliable diagnosis of HIV-1 infections. Hitherto, gp41 was solubilized by adding detergents, or in acidic or alkaline solvents. We find that covalent fusions with SlyD or FkpA, two homodimeric Escherichia coli chaperones with peptidyl-prolyl isomerase activity, solubilize retroviral envelope proteins without compromising their immunological reactivity. gp41 from HIV-1, gp36 from HIV-2 and gp21 from HTLV could be expressed in large amounts in the Escherichia coli cytosol when fused with one or two subunits of SlyD or FkpA. The fusion proteins could be easily isolated and refolded, and showed high solubility and immunoreactivity, thus providing sensitive and reliable tools for diagnostic applications. Covalent fusions with SlyD or FkpA might be valuable generic tools for the solubilization and activation of aggregation-prone proteins.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 15644217
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
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 > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 20 May 2015 09:45
Last Modified: 09 Mar 2016 14:50
URI: https://eref.uni-bayreuth.de/id/eprint/13937