Clonal Nature of the Immune Response to Phosphorylcholine

Claflin, J L; Davie, Joseph M.

doi:10.1084/jem.140.3.673

Cited by 102 publications

(28 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…determinant, H8,,, has been shown to lie in the binding site (24) and correlates precisely with binding specificity (12,13) . Therefore, antibodies raised in mice representative of all heavy chain linkage groups and myeloma proteins in the T15 group possess this determinant.…”

Section: Discussionmentioning

confidence: 99%

“…Except for some possible discrepancies (29; Claflin and Davie, unpublished observations), this determinant is found principally on anti-PC antibodies or myelomas raised in mice of the al IgC . heavy chain linkage group (16) and does not correlate with binding site specificity (15 …”

Section: Discussionmentioning

confidence: 99%

“…Calcium and cadmium ions in PC and GPC, respectively, were precipitated with phosphate before use. Chicken gamma globulin (CGG) and bovine serum albumin (BSA) were conjugated to PC as previously described (15) .…”

Section: Methodsmentioning

confidence: 99%

“…Myeloma Proteins and Anti-PC Antibodies . Myeloma proteins and mouse IgM antibodies specific for PC were isolated by affinity chromatography from a PC-Sepharose immunoadsorbent (20) as previously described (13) . CBPC 2, kindly provided by Doctors M .…”

Section: Methodsmentioning

confidence: 99%

See 3 more Smart Citations

Clonal nature of the immune response to phosphorylcholine (PC). V. Cross-idiotypic specificity among heavy chains of murine anti-PC antibodies and PC-binding myeloma proteins.

Claflin¹,

Davie²

1975

The Journal of Experimental Medicine

View full text Add to dashboard Cite

Williams et al.(1) in a study of monoclonal IgM cold agglutinins noted that antisera to different cold agglutinins possessed specificity not only for antigenic determinants unique to the individual proteins but also for determinants that were shared by cold agglutinins from a number of individuals . This phenomenon of shared or cross-idiotypy among immunoglobulins with similar specificity also has been demonstrated for human proteins with anti-7-globulin activity (2) and among rabbit (3, 4) and mouse (5) antibodies to streptococcal group carbohydrates . In most instances the proteins exhibiting cross-idiotypic reactions had similar, but not necessarily identical, combining sites, and the idiotypic determinant shared by them was associated with the combining site (2, 5-8) . Support for the structural similarity of antibodies with similar specificity and shared idiotypy has been provided by recent findings showing that IgM cold agglutinins, anti-y-globulins (9, 11), or rabbit antibodies to streptococcal group C carbohydrate (7) have strikingly similar heavy and/or light chains .Previous studies from our laboratory have demonstrated a remarkable similarity in the combining sites of mouse antibodies to phosphorylcholine (PC)' regardless of the genetic background of the mice. The antibodies from the mouse strains tested possessed indistinguishable binding specificities for a number of choline analogues (12) and had identical binding-site antigenic determinants (13) . This suggests a striking conservation of the binding site region of mouse anti-PC antibodies, even though differences have been shown to exist in other portions of the variable region (14-16) . In contrast, it was shown (17) that three PC-binding myeloma proteins that differed in combining specificity (18), as well as in idiotypes (19) and in light chains (17), have heavy chain sequences which are virtually identical through the first hypervariable region . These findings *

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Clonal nature of the immune response to phosphorylcholine (PC). V. Cross-idiotypic specificity among heavy chains of murine anti-PC antibodies and PC-binding myeloma proteins.

Claflin¹,

Davie²

1975

The Journal of Experimental Medicine

View full text Add to dashboard Cite

show abstract

“…The preparation and characterization of two idiotypic antisera which react with T15 and H8 are described in detail elsewhere (19,20,22). One antiserum, prepared in rabbits to H8, was passed over an H8-Sepharose immunoadsorbent and antibodies with specificity for the binding site were isolated by elution with PC .…”

Section: Methodsmentioning

confidence: 99%

Structural, functional, and idiotypic characteristics of a phosphorylcholine-binding IgA myeloma protein of C57BL/ka allotype.

Claflin¹,

Rudikoff²,

Potter³

et al. 1975

The Journal of Experimental Medicine

View full text Add to dashboard Cite

An IgA phosphorylcholine (PC)-binding myeloma protein with IgCH allotypic determinants different from those of BALB/c mice is characterized. The myeloma, CBPC 2, was induced in the CB-20 strain of mice which is congenic to BALB/c but differs from it by carrying the A15 allotypic determinant of C57BL/ka mice. Sequence analysis of the CBPC 2 light chain through the first hypervariable region, as well as isoelectric point analysis, show that this chain is indistinguishable from that of T15, a PC-binding myeloma protein of BALB/c origin. The heavy chains of CBPC 2 and T15 differ by only two amino acids (positions 14 and 16) through the first hypervariable region. As measured by inhibition of precipitation, both CBPC 2 and T15 have the same specificity for PC, glycerophosphorylcholine, acetylcholine, and choline. In addition, CBPC 2 possesses the binding site-associated idiotypic determinant which is present on T15. However, like normal or induced C57BL/6 anti-PC antibody, it does not possess the nonbinding site idiotypic determinant.

show abstract

Genetic marker in the variable region of kappa chains of mouse anti‐phosphorylcholine antibodies

Claflin

1976

Eur J Immunol

View full text Add to dashboard Cite

A newly discovered genetic marker in the kappa light chains of mouse immunoglobulins is described. This marker, designated kappa-PC8, is located in the L chains of those anti-phosphorylcholine (PC) antibodies which show the same functional and idiotypic characteristics as a PC-binding myeloma protein, HOPC 8 (H8). Analytical isoelectric focusing of these L chains revealed two phenotypes whose strain distribution pattern suggested a genetic association with genes that determine the T lymphocyte surface antigen(s) Ly-2/Ly-3. In four strains , AKR/J, C58/J, RF/J and PL/J (AKR-type, A) the H8-like L chains have a slightly lower isoelectric point than those of C57L/J and 12 other strains (C57L-type, B). Breeding experiments showed that the kappa-PC8-A phenotype is preferentially expressed. The most probable location of the marker is the variable region since other idiotypically related kappa-chains in C57L/J and AKR/J do not show differences in their electrophoretic mobility.

show abstract

Clonal Nature of the Immune Response to Phosphorylcholine

Cited by 102 publications

References 35 publications

Clonal nature of the immune response to phosphorylcholine (PC). V. Cross-idiotypic specificity among heavy chains of murine anti-PC antibodies and PC-binding myeloma proteins.

Clonal nature of the immune response to phosphorylcholine (PC). V. Cross-idiotypic specificity among heavy chains of murine anti-PC antibodies and PC-binding myeloma proteins.

Structural, functional, and idiotypic characteristics of a phosphorylcholine-binding IgA myeloma protein of C57BL/ka allotype.

Genetic marker in the variable region of kappa chains of mouse anti‐phosphorylcholine antibodies

Contact Info

Product

Resources

About