T helper cell recognition of idiotopes on lambda 2 light chains of M315 and T952: evidence for dependence on somatic mutations in the third hypervariable region.

Previous work has indicated that BALB/c T helper cells (Th) recognize an idiotope expressed on a 88-114/117 fragment of V lambda 2 of BALB/c myeloma protein 315. In the present study the antigenic structure of this idiotope was further analyzed. Conventional carrier-specific Th elicited by immunization of BALB/c mice with free lambda 2(315) did not cross-react with the free lambda 2 chain of the BALB/c myeloma protein T952 which differs from lambda 2(315) in five amino acid positions (38, 94, 95, 96, 99).

H-2-linked Ir genes have a striking influence on the immunogenicity of idiotopes of myeloma protein 315 for T helper cells.

H-2-linked immune response (Ir) genes control T helper cells (Th) that recognize idiotopes of the V domains of myeloma protein 315 as carriers; Th recognition was detected by augmentation of antibody responses of hapten (4-hydroxy-3-iodo-5-nitrophenylacetyl (NIP]-primed B cells boosted with NIP conjugated to Fab315. The present study indicates that the responder k allele of the Ir VH315 gene maps to the I-A subregion of H-2. A responder s allele of the Ir V lambda 2(315) gene on an A-strain background was identified, which also most likely maps to I-A.

Antibody responses to lambda 1J558 and lambda 2315 light chains. Specificity and genetic regulation.

Specificity of BALB/c antibody responses to lambda chains of isologous myeloma proteins 315 and J558 was explored by enzyme-linked immunosorbent assay. lambda-chain binding antibodies were not detected when immunizing with assembled (H + L) myeloma proteins. However, relatively high titred IgG antibodies were elicited by free lambda 2(315) immunization.

Specificity of antibody and helper T-cell responses to the isologous myeloma protein W3129 and its subunits.

The specificity of BALB/c antibodies and Th elicited by BALB/c myeloma protein W3129 (alpha, kappa) and its subunits was studied. Antibodies were detected with RIA and ELISA techniques. Th were demonstrated by their ability to augment a secondary anti-NIP antibody response in a Mitchison type assay of adoptive immunity.

Determinant-specific regulation of T helper cell responses to murine lambda light chains by both H-2 and non-H-2 genes.

Previous work has revealed that the T helper cell (Th) responses to an antigenic determinant of V lambda 2(315) (called lambda 2.1) is regulated by both H-2 and non-H-2 genes. In the present study this was confirmed and extended to two other determinants, one shared between free lambda 2(315) and lambda 1(J558) (called lambda 2.

T helper cells recognize an idiotope located on peptide 88-114/117 of the light chain variable domain of an isologous myeloma protein (315).

Isolated variable region light chain 315 (VL-315), the VL domain of a myeloma protein of BALB/c origin, induces T cells of BALB/c (H-2d) mice that help the adoptive secondary anti-4-hydroxy-3-iodo-5-nitrophenylacetyl (NIP) antibody response to NIP-Fab315. The location of the epitope recognized by helper cells was examined with two fragments of VL-315, obtained by cleavage with cyanogen bromide at Met 87. Both N-terminal fragment 1-86 and C-terminal fragment 88-114/117 elicited BALB/c antibodies that bound to the respective fragments and to VL-315.

Recognition of lambda 1 and lambda 2 murine light chains by carrier-specific isologous T helper cells; effect of L-H chain assembly.

Previous studies from this laboratory have revealed an antigenic site located on the variable domain of the lambda 2 light chain of BALB/c myeloma protein 315 (the V lambda 2(315) site). This site is recognized by conventional carrier-specific T helper cells (Th) of BALB/c mice and is expressed on both the free and assembled V lambda 2(315) domain. The present work defines two new antigenic sites associated with murine lambda chains.

Monoclonal hybridoma antibodies to human amyloid related protein SAA.

Problems concerning isolation and characterization of the amyloid related serum protein SAA in a pure form prompted us to make monoclonal antibodies to the protein. Protein SAA isolated by gel filtration under dissociating conditions was used for immunization of BALB/c mice, and spleen cells from a mouse producing high titred antiserum to SAA were fused with cells from the mouse plasmacytoma line P3U1. Antibody specificity to various preparations of protein SAA was tested using an indirect enzyme-linked immunosorbent assay.

A computer-generated catalog of audiovisuals.

A computer-generated catalog of nonprint media is described. Examples are given of four access points to the data base: (1) main entry, (2) title, (3) MeSH terms, and (4) broad subject categories. The data input procedure is summarized.