Modified immunoglobin molecules and methods for use thereof

Details Modified immunoglobin molecules and methods for use thereof Modified immunoglobin molecules and methods for use thereof

1999-04-20

2001-09-04

Park, Hankyel T. (Department: 1648)

Chemistry: molecular biology and microbiology

Animal cell, per se ; composition thereof; process of...

Animal cell, per se, expressing immunoglobulin, antibody, or...

C435S005000, C435S007100, C435S069700, C435S070100, C435S320100, C435S339100, C530S387300, C536S023400, C424S133100, C424S160100, C424S161100

Reexamination Certificate

active

06284536

ABSTRACT:

Throughout this application various publications are referenced. The disclosures of these publications in their entireties are hereby incorporated by reference into this application in order to more fully describe the state of the art to which this invention pertains.
TECHNICAL FIELD OF THE INVENTION
The invention relates to modified immunoglobulin molecules comprising at least a portion of a domain of an immunoglobulin (Ig) of a first class and at least a portion of an immunoglobulin of a second class. In a preferred embodiment, the first Ig is of the IgA class. The domain of the Ig molecule is typically a constant domain. Modified Ig molecules comprising portions of different immunoglobulin classes can be used in the diagnosis, prevention and treatment of infection and other diseases.
BACKGROUND OF THE INVENTION
The design of modified immunoglobulin molecules makes it possible to overcome the limitations of naturally-occurring antibodies. Chimeric antibodies having an antigen-binding region derived from a murine source and constant regions of human origin are described, for example, in Neuberger et al., 1985, Nature 314:268-270; and Bouhanne et al., 1984, Nature 312:643. Antibodies having constant regions modified to contain domains of different IgG isotypes are described in WO 89/07142.
There remains a need for immunoglobulin molecules offering desired features characteristic of one Ig class in combination with desired features characteristic of another Ig class. In addition, information about which domains of Ig molecules confer the desired features is needed to guide in the design of modified Ig molecules.
SUMMARY OF THE INVENTION
The invention provides a modified immunoglobulin molecule comprising a constant domain of an IgA molecule, and at least a portion of a nonIgA immunoglobulin molecule. In one embodiment, the constant domain is a C
H
1, C
H
2 and/or C
H
3 domain. In one embodiment, the portion of a nonIgA immunoglobulin molecule comprises a C
H
2 domain. The nonIgA immunoglobulin molecule can be an IgG, IgM, IgE, or IgD molecule. In one embodiment, the modified Ig molecule further comprises a tail-piece region of an IgA immunoglobulin molecule, a J chain, and/or secretory component (SC).
The invention additionally provides polynucleotides encoding a modified immunoglobulin molecule, vectors and host cells which can be used in a method of producing a modified immunoglobulin molecule.
The invention also provides a pharmaceutical composition comprising the modified immunoglobulin molecule and, optionally, a pharmaceutically acceptable carrier. The composition can be used in a method of treating or preventing an infection in a subject. The method comprises administering the composition to the subject. The infection to be treated or prevented can be systemic, local, or at a mucosal surface.


REFERENCES:
patent: WO 89/07142 (1989-01-01), None
patent: WO 97/42313 (1997-11-01), None
Atkin, J.D. et al., “Mutagenesis of the Human IgA1 Heavy Chain Tailpiece That Prevents Dimer Assembly1”, Jul. 1, 1996, J. Immunol., 157(1):156-159.
Boulianne et al., “Production of Functional Chimaeric Mouse/Human Antibody”, Dec. 13, 1984, Nature, 312:643.
Carayannopoulos, L. et al., “Localization of the Binding Site for the Monocyte Immunoglobulin (Ig) A-Fc Receptor (CD89) to the Domain Boundary Between C&agr; and C&agr;3 in Human IgA1”, Apr. 1996, J. Exp. Med., 183:1579-1586.
Chintalacharuvu and Morrison, “Residues Critical for H-L Disulfide Bond Formation in Human IgA1 and IgA21”, Oct. 15, 1996, J. Immunol., 157:3443-49.
Krugmann, S. et al., “Mutagenesis of J Chain Residues Critical for IgA Dimer Assembly”, May 1997, Biochem. Soc. Trans 25(2):323S.
Morrison et al., “Chimeric Human Antibody Molecules: Mouse Antigen-binding Domains with Human Constant Region Domains”, Nov. 1984, PNAS, USA, 81:6851-6855.
Neuberger et al., “A Hapten-specific Chimeric IgE Antibody with Human Physiological Effector Function”, Mar. 1985 Nature, 314:268-270.
Niles, M.J. et al., “Polymer IgM Assembly and Secretion in Lymphoid and Nonlymphoid Cell Lines: Evidence that J Chain is required for Pentamer IgM Synthesis”, Mar. 1995, Proc. Natl., Acad. Sci., USA, 92:2884-2888.
Wiersma, E.J. et al., “Analysis of IgM Structures Involved in J Chain Incorporation1”, Feb. 15, 1997, J. Immunol. 158(4):1719-1726.
Ma, Julian K.C. et al., “Generation and Assembly of Secretory Antibodies in Plants,” Science, May 5, 1995, vol. 268, pp. 716-719.
Sorensen, Vigdis et al., “Effect of the IgM and IgA Secretory Tailpieces on Polymerization and Secretion of IgM and IgG,” Journal of Immunology, 1996, 156: 2858-2865.
Smith, Richard I.F. et al., “Addition of a &mgr;-Tailpiece to IgG Results in Polymeric Antibodies with Enhanced Effector Functions Including Complement-Mediated Cytolysis by IgG4,” Journal of Immunology, 1995, 154: 2226-2236.
Clarke, R.A. et al., “Expression of a Recombinant Sheep IgE Gene,” Immunological Investigation, 1994, 23(1), 25-37.

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