Abstract:
:We previously showed that a variety of amino acid substitutions at positions 58 and 59 in the V(H) CDR2 of an anti-arsonate (Ars) antibody Fab simultaneously resulted in increased or unaltered affinity for Ars and substantially enhanced affinity for DNA. To test the generality of these observations, we generated and characterized several antibody phage display libraries of this Fab containing random amino acid substitutions at V(H) CDR2 position 55. Position 55 was randomized in two contexts; in the unmutated V region, and in a previously isolated V(H) CDR2 position 58 and 59 mutant that displayed binding to both Ars and ssDNA. In the unmutated V region context, mutants that displayed strong binding to both Ars and DNA nearly exclusively contained Arginine residues at position 55. In the context of the 58 and 59 mutations, a variety of amino acid residues were observed at position 55 among mutants that bound strongly to both Ars and DNA, including Arginine, Lysine and Serine. None of these position 55 mutations measurable altered affinity for Ars. These data substantiate the view that "dual reactive" antibodies--specific for both a foreign and an autoantigen--are frequently generated in vivo via hypermutation during immune responses driven by the foreign antigen.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Hande S,Manser Tdoi
10.1016/s0161-5890(98)00005-4subject
Has Abstractpub_date
1997-12-01 00:00:00pages
1281-90issue
18eissn
0161-5890issn
1872-9142pii
S0161589098000054journal_volume
34pub_type
杂志文章abstract::In the host a diverse collection of endogenous danger signals is constantly generated consisting of waste material as protein aggregates or crystalline materials that are recognized and handled by soluble pattern recognition receptors and phagocytic cells of the innate immune system. These signals may under certain ci...
journal_title:Molecular immunology
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pub_type: 杂志文章
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pub_type:
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更新日期:2003-01-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章,评审
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更新日期:2017-04-01 00:00:00
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pub_type: 杂志文章
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