Modulation of fine specificity of anti-DNA antibody by CDR3L residues

Jang, Young-Ju; Sanford, David G.

doi:10.1016/s0161-5890(01)00066-9

Cited by 8 publications

(6 citation statements)

References 14 publications

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“…For example, the VH domain of mAb Z22 (13), dC7 (3), and 2C10 (7) bound to ds-Z-DNA, ss-(dC) 65 , and ds-DNA, respectively, whereas their respective VL domains alone did not bind to the substrates. Thus it has been proposed that VL alone could not bind to DNA, but instead modulates fine specificities and affinities of VH binding to DNA (2,3,7,15,38). However, our results demonstrated that 3D8 VL alone bound to ss-and dsDNAs of various sequences.…”

Section: Figurementioning

confidence: 99%

Heavy and Light Chain Variable Single Domains of an Anti-DNA Binding Antibody Hydrolyze Both Double- and Single-stranded DNAs without Sequence Specificity

Kim

Lee

et al. 2006

Journal of Biological Chemistry

103

152

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Section: Figurementioning

confidence: 99%

Heavy and Light Chain Variable Single Domains of an Anti-DNA Binding Antibody Hydrolyze Both Double- and Single-stranded DNAs without Sequence Specificity

Kim

Lee

et al. 2006

Journal of Biological Chemistry

103

152

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“…The notion that specific LC residues can serve to contact DNA directly is further supported by site-directed mutagenesis studies. For instance, other investigators (52,53) have demonstrated that mutating away particular D residues in LC CDR1 can augment DNA binding. Although the roles of different LCs and specific LC residues have been elegantly demonstrated by the above transfection, transgenic, and mutagenesis studies, the potential role that any such differences might play in spontaneously arising ANAs remains unclear.…”

mentioning

confidence: 99%

Molecular Signatures of Anti-nuclear Antibodies: Contributions of Specific Light Chain Residues and a Novel New Zealand BlackVκ1Germline Gene

Liang

Mohan

2003

The Journal of Immunology

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Although the Ig H chains of anti-nuclear Abs (ANA) have been described to possess certain shared molecular signatures, it remains unclear whether the L chains of these Abs also possess distinctive molecular features. The present study examines this by generating and analyzing two comprehensive murine Ig L chain databases, one consisting of 264 monoclonal ANAs and the other consisting of 145 non-ANAs, drawn from previously published work. Importantly, clonal replicates were represented only once each, so as to minimize bias. ANAs and non-ANAs did not differ in Vκ family or Jκ gene usage, nor in their mutation frequencies. Interestingly, the L chains of ANAs exhibited differential usage of certain complementarity-determining region residues, arising almost entirely from the increased usage of certain Vκ germline genes, notably, Vκ ai4 among anti-dsDNA ANAs, Vκ23–45 among anti-ssDNA ANAs, and Vκ21–12 among non-ANAs. Finally, prompted by the increased prevalence of a particular Vκ1 family sequence among ANAs, we proceeded to clone a novel New Zealand Black Vκ1 germline gene, named bb1.1, which appears to be frequently used to encoded anti-ssDNA Abs. Collectively, these studies underline the potential contribution of particular Vκ germline genes in promoting or thwarting DNA binding.

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“…In contrast, the amino acid sequence of the V L region was identical to that of the monoclonal antibody for a human tumor-associated antigen but not that of anti-DNA antibodies. It has been reported that the light chain modulates the specificity of the antibody in DNA-binding (26) and that the amino acid sequences act as a peptide of mimic of DNA (18,19) ; hence, the epitope of the human tumorassociated antigen might function the same as DNA in binding to D-1-1 antibody. Because scFv of D-1-1 reacted with DNA fragments (Fig.…”

Section: Discussionmentioning

confidence: 99%

Preparation and Characterization of an Anti-DNA Monoclonal Antibody Showing Size Selectivity Toward DNA Fragments

Onishi

Kato

Hanyu

2004

Hybridoma and Hybridomics

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Anti-DNA monoclonal antibodies were prepared using an in vitro immunization method. Balb/c mouse splenocytes were immunized with HeLa cell nuclear extract in the presence of N-acetylmuramyl-L-alanyl-D-isoglutamine and fused with P3U1 myeloma cells using PEG 4000. After HAT selection and ELISA using fragmented HeLa genomic DNA, an anti-DNA monoclonal antibody was obtained. The monoclonal antibody D-1-1, whose isotype was IgM, interacted with a variety of double-stranded DNA. The antibody reacted only with DNA fragments longer than 0.8 kbp, and its apparent dissociation constant for a 1.0-kbp DNA fragment was 34 nM. This antibody will be a helpful tool for the detection of DNA structures.

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Modulation of fine specificity of anti-DNA antibody by CDR3L residues

Cited by 8 publications

References 14 publications

Heavy and Light Chain Variable Single Domains of an Anti-DNA Binding Antibody Hydrolyze Both Double- and Single-stranded DNAs without Sequence Specificity

Heavy and Light Chain Variable Single Domains of an Anti-DNA Binding Antibody Hydrolyze Both Double- and Single-stranded DNAs without Sequence Specificity

Molecular Signatures of Anti-nuclear Antibodies: Contributions of Specific Light Chain Residues and a Novel New Zealand BlackVκ1Germline Gene

Preparation and Characterization of an Anti-DNA Monoclonal Antibody Showing Size Selectivity Toward DNA Fragments

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