J. Donald Capra

Judith and Jean Pape Adams Charitable Foundation

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J. Michael Kehoe

Northeast Ohio Medical University

Philip W. Tucker

Swansea University

Richard G. Cook

University of Tennessee at Chattanooga

Ellen S. Vitetta

The University of Texas Southwestern Medical Center

Patrick C. Wilson

Cornell University

Grant R. Kolar

Saint Louis University

Virginia Pascual

Weill Cornell Medicine

Jonathan W. Uhr

The University of Texas Southwestern Medical Center

J W Uhr

New York University

Richard D. Sontheimer

University of Utah

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The University of Texas Southwestern Medical Center

105

Oklahoma Medical Research Foundation

Southwestern Medical Center

University of Texas Health Science Center at Dallas

National Institutes of Health

Cornell University

University of Oklahoma Health Sciences Center

Icahn School of Medicine at Mount Sinai

Harvard University

The University of Texas Health Science Center at Houston

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Immunoglobulin heavy chain variable region gene usage in human autoimmune diseases

Advances in experimental medicine and biology (1995)

Virginia Pascual J. Donald Capra

Immunoglobulin gene

Immunoglobulin heavy chain

Gene conversion

Gene rearrangement

V(D)J recombination

Immunoglobulin D

10.1007/978-1-4613-0331-2_11

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Citations (7)

Structural studies on the murine ia alloantigens—III.

Molecular Immunology (1979)

Richard G. Cook Ellen S. Vitetta Jonathan W. Uhr J. Donald Capra

Congenic

10.1016/0161-5890(79)90024-5

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Citations (47)

Common Structural Features Among the Light Chains of γG and γM Anti-γ Globulins

The Journal of Immunology (1971)

J. Donald Capra J. Michael Kehoe

Abstract Benign hypergammaglobulinemic purpura is characterized by a marked elevation of the γ globulin level which on serum protein electrophoresis is broadbased and only rarely has the appearance of an M component. Anti-γ globulins of the γG type were isolated from these sera using specific absorption on BDB cross-linked γ globulin followed by acid elution. Extensive studies on 4 eluates and more limited studies on 12 other sera provided evidence that these anti-γ globulins had restricted heterogeneity in the great majority of cases. The light chains (VκI) of two γG anti-γ globulins were sequenced to residue 40 and were identical. Two VκIII light chains derived from γM anti-γ globulins were also sequenced to residue 40, all four proteins had a serine residue at position 31 the most variable of all positions in κ light chains except for position 96. Only one other κ chain has been described with a serine in this position.

Residue (chemistry)

10.4049/jimmunol.107.3.925.b

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Citations (3)

Structural characterization of antiidiotypic antibodies. Evidence that Ab2s are derived from the germline differently than Ab1s.

The Journal of Experimental Medicine (1989)

K Meek Charles A. Hasemann Brian A. Pollok Ş. Ş. Alkan Maryse Brait

We have found that syngeneic Ab2s in the antiarsonate system are serologically and structurally similar to one another. In contrast, the allogeneic Ab2 response is heterogeneous and derives from a large number of unrelated germline gene segments. The Ab2 response of the BALB/c strain to polyclonal A/J Ars A molecules can probably best be compared with a response to a foreign protein and might have been predicted in a strain that completely lacks the H chain V region gene from which the Ab1 derives. Partial variable region sequences of Ab2s from three other systems in addition to previously reported Ab2 structures indicates that this difference in allogeneic vs. syngeneic Ab2s may be a general phenomena. These data support Jerne's hypothesis of complementary V region genes existing in the germline. However, there is good evidence that these antiidiotypic antibodies are not derived directly from the germline, as somatic processes most likely play an important role in their generation. The D segments of Ab2s in the arsonate system as well as in other systems, are novel in structure and cannot easily be explained by previously described germline D segments. D-D fusion may play a role in the generation of the third hypervariable region in these antibodies.

Hypervariable region

Polyclonal antibodies

Immunogenetics

10.1084/jem.169.2.519

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Citations (20)

Biased VH4 Gene Segment Repertoire in the Human Tonsil

KARGER eBooks (1997)

Virginia Pascual Peter J. Wilson Y.J. Liu Jacques Banchereau J. Donald Capra

Tonsil

10.1159/000058677

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Citations (13)

Structural Studies on Induced Antibodies with Defined Idiotypic Specificities

The Journal of Immunology (1975)

J. Donald Capra Amar S. Tung Alfred Nisonoff

Abstract N-terminal amino acid sequence analyses have been performed on three preparations of light chains of A/J mice. Light chains derived from the IgG of unimmunized animals were compared to light chains of anti-p-azophenylarsonate (anti-Ar) antibodies possessing a cross-reacting idiotype (CRI); the latter were derived from the ascites fluid of a single A/J mouse, or from the pooled ascites fluids of 18 A/J mice. The heavy chains of these same two antibody preparations had previously been shown to comprise a single, homogeneous sequence to position 40. With few exceptions, the first 26 positions of light chains derived from unimmunized animals were extremely heterogeneous; the heterogeneity is comparable to that observed in a composite of sequence data on light chains of BALB/c myeloma proteins. Although the light chains obtained from anti-Ar antibodies possessing the CRI (whether from the pool of 18 A/J mice or from a single mouse) were more restricted in their sequence, at several positions as many as four alternative amino acids were detected. These studies indicate that an antibody population with defined idiotypic specificity, and very possibly identical heavy chain sequences, may contain at least four distinct light chains. The feasibility of structural studies on antibodies induced in individual mice is further demonstrated.

Myeloma protein

Sequence (biology)

10.4049/jimmunol.115.2.414

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Citations (57)

Immunoglobulin variable region gene segments in human autoantibodies

Elsevier eBooks (1995)

Kathleen N. Potter J. Donald Capra

Antibody Repertoire

Immunoglobulin gene

10.1016/b978-012053640-5/50020-3

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