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A spontaneous variant of an antidigoxin hybridoma antibody with increased affinity arises from a heavy chain signal peptide mutation.

Abstract：

:The A/J murine hybridoma cell line 40-150 secretes antidigoxin antibodies with high affinity for digoxin. A first-order spontaneous mutant (40-150 A2.4) produces antibodies containing a mutation at heavy chain position 94 resulting in reduced affinity for digoxin. A second-order mutant (40-150 A2.4 P.10) derived from 40-150 A2.4 produces two species of antibody: one identical to 40-150 A2.4 and the other with a two amino acid truncation at the heavy chain amino-terminus [Panka et al., Proc. natn. Acad. Sci. U.S.A. 85, 3080-3084 (1988)]. The truncated antibody has increased affinity for digoxin relative to the nontruncated variant. Direct nucleotide sequence analysis of polymerase chain reaction amplified heavy chain variable region cDNA derived from 40-150 A2.4 P.10 reveals a point mutation at the -2 position of the signal peptide, resulting in a glutamine to proline change. Southern blots of genomic DNA from all three cell lines gave identical patterns and were consistent with a single heavy chain mRNA derived from a single rearranged gene. The presence of proline at the heavy chain -2 position of antibody 40-150 A2.4 P.10 partially shifts the cleavage site of the signal peptidase to the +2 position, resulting in the production of both full-length and truncated antibody heavy chains. Signal peptide mutation resulting in a change in antibody affinity for antigen is a hitherto unidentified possible mechanism for antibody diversification.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Shaw SY,Margolies MN

doi

10.1016/0161-5890(92)90010-u

subject

Has Abstract

pub_date

1992-04-01 00:00:00

pages

525-9

issue

4

eissn

0161-5890

issn

1872-9142

journal_volume

29

pub_type

杂志文章

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