Variable region primary structures of monoclonal anti-DNA autoantibodies from NZB/NZW F1 mice

Molecular Immunology
R G Smith, E W Voss

Abstract

VH and VL region primary structures of five NZB/NZW F1 derived monoclonal anti-DNA autoantibodies were determined from cloned cDNA. Comparative analysis of VH genes showed that except for two VH genes that shared complete identity the overall VH gene usage was diverse. Comparison of VH genes with those utilized in a variety of antibody responses showed they were generally unique to the autoanti-DNA response although framework homologies allowed assignment of four of five VH genes to existing murine heavy chain gene families. Only one out of five D segments shared homology to existing germline D segments, and all were rearranged to JH3. V kappa genes showed restriction for four of five light chains to the V kappa 1 subgroup. The V kappa 1 subgroup has been shown previously to be utilized in several anti-DNA autoantibodies as well as a variety of antibodies to exogenous antigens. H and L chain amino acid residues associated with the active site of a ssDNA specific autoantibody, 04-01, are discussed based on recently obtained crystallographic data.

References

Dec 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·F SangerA R Coulson
Jun 12, 1989·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·A B EdmundsonE W Voss
Apr 1, 1987·Immunological Investigations·G KroemerR Kofler
Jul 1, 1985·The Journal of Experimental Medicine·R KoflerA N Theofilopoulos
Oct 1, 1988·Immunological Reviews·M ZoualiR S Schwartz
Jun 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·S M Behar, M D Scharff
Jun 1, 1988·Annals of Internal Medicine·E M Tan
Dec 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·M J ShlomchikM G Weigert
Jan 1, 1985·Advances in Immunology·A N Theofilopoulos, F J Dixon
Apr 1, 1985·European Journal of Immunology·D EilatA Zlotnick
Jan 1, 1980·Methods in Enzymology·B D Stollar
Sep 9, 1983·Science·Y TakedaB W Matthews
Jan 1, 1982·The Journal of Experimental Medicine·Y Kurosawa, S Tonegawa
Jan 1, 1980·The American Journal of Medicine·J D Clough, R Valenzuela
Aug 24, 1999·Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association·C BanotaiJ J Pestka
Jan 1, 1987·Immunology Today·R KoflerA N Theofilopoulos

❮ Previous
Next ❯

Citations

May 6, 1999·European Journal of Immunology·M S BynoeB Diamond
Jan 1, 1994·Immunologic Research·M H FosterM P Madaio
Dec 1, 1994·Immunology and Cell Biology·N R Sinclair, C C Anderson
Aug 16, 1994·Proceedings of the National Academy of Sciences of the United States of America·K N KasturiC A Bona
Aug 1, 1992·Immunological Reviews·T N MarionR J Hill
Apr 5, 1997·Annals of the New York Academy of Sciences·G Dighiero
Apr 1, 1996·The Journal of Clinical Investigation·P C SwansonG D Glick
Nov 20, 1998·The Journal of Clinical Investigation·R R SinghF M Ebling
May 20, 1998·Journal of Molecular Recognition : JMR·C J WorkmanE W Voss
Apr 1, 1993·Immunological Investigations·T A BanksR Kibler
Feb 8, 2020·Life Science Alliance·Monika A ZelazowskaKevin M McBride
Nov 25, 2003·The Journal of Immunology : Official Journal of the American Association of Immunologists·Amanda M GuthLawrence J Wysocki
Jun 5, 2008·Langmuir : the ACS Journal of Surfaces and Colloids·An-Chi ShuTri-Rung Yew

❮ Previous
Next ❯

Related Concepts

Related Feeds

Antibody Specificity

Antibodies produced by B cells are highly specific for antigen as a result of random gene recombination and somatic hypermutation and affinity maturation. As the main effector of the humoral immune system, antibodies can neutralize foreign cells. Find the latest research on antibody specificity here.