Roche Diagnostics Gmbh

Roche Diagnostics Operations, Inc.

Boehringer Mannheim Gmbh

F. Hoffmann-la Roche Ag

Urban Schmitt

Elke Faatz

Peter Schaarschmidt

Christian Scholz

Christoph Seidel

Ursula-Henrike Wienhues

Michael Wiedmann

Barbara Upmeier

Manfred Motz

Rolf Deeg

Erwin Soutschek

Richard Engh

Dittmar Schlieper

Eberhard Maurer

Wolfgang Rudinger

Rainer M&uuml;ller

Hans Brandstetter

Arno Deger

Erhard Kopetzki

Joachim Ziegenhorn

Herbert Andres

Ursula-Henrike Wienhues-Thelen

Alfred Engel

Volker Klemt

Hans-Georg Ihlenfeldt

Ariuna Bazarsuren

Wolfgang Kraas

Cristoph Seidel

Helmut Lenz

Hartmut Duefel

Gunter Pappert

Beatus Ofenloch-Hahnle

Eva Höss

Alexander Riedel

Wolf D Engel

Thomas Geiger

Franz Schmid

Gertraud Ehrlich-Weinreich

Gunther-Gerhard Jung

Christian Schotz

G&uuml;nther-Gerhard Jung

Eberhard Kopetzki

Peter Shaarschmidt

The invention concerns a fusion polypeptide including several molecules of folding helper polypeptides, including one multimerization domain, in particular Skp, and at least one molecule of SlyD or SlpA, wherein no further target polypeptide sequences are fused to the fusion polypeptide. The invention further concerns an immunoassay and the use of the fusion polypeptide in an immunoassay for reduction of interferences or minimizing false positive results or for stabilizing proteinaceous assay reagents. Further the invention concerns a reagent kit for use in an immunoassay comprising the fusion polypeptide.

Chaperone-chaperone fusion polypeptides for reduction of interference and stabilization of immunoassays

The invention relates to a method for detecting antibodies against the TpN17 antigen ofin an isolated sample wherein a peptide sequence oflipoprotein 15 (VcLp15) or a partial sequence thereof is used as a reagent for reduction of interference, i.e. for minimizing false positive results. In addition the invention relates to fusion polypeptides comprising a VcLp15 peptide sequence and a chaperone, to their use as an additive in an immunoassay for said reduction of interferences and for minimizing false positive results and to a reagent kit for detecting antibodies againstantigens in an isolated sample comprising a TpN17 antigen and said VcLp15-chaperone fusion polypeptide.

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The invention concerns soluble variants ofantigen 47 (TpN47 antigen) comprising at least domain B, or at least domains A and B, optionally domain D of the complete TpN47 protein molecule with the proviso that all antigens lack domain C (amino acid residues 224 to 351) of TpN47. The Tpn47 antigens can be fused to a chaperone. Moreover, the invention covers DNA encoding the antigens, a method of producing these antigens as well as the use of these antigens in an immunodiagnostic assay for the detection of antibodies againstin an isolated sample.

Soluble immunoreactive treponema pallidum TpN47 antigens

The present invention relates to fusion proteins suitable as test antigens in the detection of infections with pathogens, particularly of primary infections with pathogens. Further, the invention relates to methods for detecting and differentially determining antibodies, particularly IgM antibodies resulting from an infection with a pathogenic organism. Furthermore, test reagents for carrying out these methods are provided.

Detection of primary infections with pathogens

Disclosed are a recombinant DNA molecule encoding a fusion protein comprising a SlpA chaperone and a target polypeptide wherein human FK506 binding proteins (FKBPs) are excluded as target polypeptides, a corresponding expression vector encoding said fusion protein as well as host cells transformed with said expression vector. Also disclosed are a method for producing the fusion protein, a recombinantly produced fusion protein comprising a SlpA chaperone and a target polypeptide. A further aspect of the invention is the use of the recombinantly produced fusion protein, and a reagent kit containing a recombinantly produced fusion protein comprising a SlpA chaperone and a target polypeptide.

SlpA as a tool for recombinant protein and enzyme technology

The present invention relates to the cloning and expression of foreign protein or polypeptides in bacteria, such as. In particular, this invention relates to expression tools comprising a FKBP-type peptidyl prolyl isomerase selected from the group consisting of FkpA, SlyD, and trigger factor; methods of recombinant protein expression, the recombinant polypeptides thus obtained, as well as to the use of such polypeptides.

Methods for producing fusion polypeptides or enhancing expression of fusion polypeptides

The invention discloses the cloning, expression and uses of a chimeric fusion protein with superior chaperone and folding activities compared to the wild type chaperones. This invention relates to a chimeric fusion protein encoded by a recombinant DNA molecule containing nucleotide sequences coding for a polypeptide binding segment of a non-human chaperone protein and nucleotide sequences coding for an FK506 binding protein (FKBP) or an FK506-binding-protein-like domain (FKBP-like domain). In particular, this invention relates to a chimeric fusion protein encoded by a recombinant DNA molecule containing nucleotide sequences coding for a polypeptide binding segment of a non-human chaperone protein and nucleotide sequences coding for a human FKBP type peptidyl-prolyl-cis/trans isomerase (PPIase), methods of producing these chimeric fusion proteins and their uses as folding helpers in the production of other proteins and in the process of the production of vaccines or pharmaceuticals, and as folding helpers for performing immunoassays.

The invention discloses the cloning, expression and uses of a chimeric fusion protein with superior chaperone and folding activities compared to the wild type chaperones. This invention relates to a chimeric fusion protein encoded by a recombinant DNA molecule comprising nucleotide sequences coding for a polypeptide binding segment of a non-human chaperone protein and nucleotide sequences coding for an FK506 binding protein (FKBP) or an FK506-binding-protein-like domain (FKBP-like domain). In particular, this invention relates to a chimeric fusion protein encoded by a recombinant DNA molecule comprising nucleotide sequences coding for a polypeptide binding segment of a non-human chaperone protein and nucleotide sequences coding for a human FKBP type peptidyl-prolyl-cis/trans isomerase (PPIase), methods of producing these chimeric fusion proteins and their uses as folding helpers in the production of other proteins and in the process of the production of vaccines or pharmaceuticals, and as folding helpers for performing immunoassays.

The present invention relates to the cloning and expression of foreign protein or polypeptides in bacteria, such asIn particular, this invention relates to expression tools comprising a FKBP-type peptidyl prolyl isomerase selected from the group consisting of FkpA, SlyD, and trigger factor; methods of recombinant protein expression, the recombinant polypeptides thus obtained, as well as to the use of such polypeptides.

Fusion polypeptides, vaccines and compositions of FKBP chaperones and target polypeptides

The present invention concerns a polypeptide which is composed of the amino acids 1207&#xb1;10 to 1488&#xb1;10 of a hepatitis C virus and of less than 20 foreign amino acids and the use of this polypeptide as an antigen in an immunological test.

Method for determining early HCV seroconversion

The invention concerns a method for the determination of antigen-specific antibodies of the immunoglobulin G class in the presence of immunoglobulins of the M class in body fluids by incubation with at least two different receptors R and R and optionally additional receptors, an essential component of R being a binding partner in monomeric form, a reagent for determining an antigen-specific antibody of the immunoglobulin G class as well as the use of binding partners in monomeric form for the determination of an antigen-specific antibody of the immunoglobulin G class.

Antigen-specific IgG detection

The invention concerns a method for the determination of antigen-specific antibodies of the immunoglobulin M class in the presence of immunoglobulins of the G class and/or rheumatoid factors in body fluids by incubation with at least two different receptors R and R and optionally additional receptors wherein an essential component of R is a binding partner in a polymeric form and interference by IgG antibodies of the same antigen specificity is reduced by binding partners in a monomeric form; a reagent for determining an antigen-specific antibody of the immunoglobulin M class, as well as the use of binding partners in a monomeric form to reduce interference by IgG antibodies in the determination of antigen-specific IgM antibodies.

Antigen-specific IgM detection

The invention concerns a method for typing antibodies in a sample liquid by means of type-specific antigens and in particular a method for typing antibodies to the hepatitis C virus and peptide antigens suitable for this.

Method for serological typing using type-specific antigens

The present invention concerns muteins of avidin and streptavidin with a reduced binding affinity for biotin as well as their use as interference elimination reagents in methods for the determination of an analyte e.g. in diagnostic tests such as for example immunoassays and nucleic acid hybridization assays. In addition the invention concerns the use of muteins of avidin and streptavidin as systems capable of regeneration for binding biotin e.g. for the analysis of biotinylated molecules, for examining receptor ligand interactions as well as for the affinity purification of biotinylated molecules.

Recombinant inactive core streptavidin mutants

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Kochel, Germany

Urban Schmitt