Presence of Catalytic Activity of the Antibody Light Chain Raised against Complementarity Determining Region Peptide of Super Catalytic Antibody

2002 ◽  
pp. 200-208 ◽  
Author(s):  
Y. Zhou ◽  
E. Hifumi ◽  
H. Kondo ◽  
T. Uda
Keyword(s):  
Catalytic Activity ◽  
Light Chain ◽  
Catalytic Antibody ◽  
Complementarity Determining Region

scholarly journals A new algorithm to convert a normal antibody into the corresponding catalytic antibody

2020 ◽  
Vol 6 (13) ◽  
pp. eaay6441
Author(s):  
Emi Hifumi ◽  
Hiroaki Taguchi ◽  
Haruna Tsuda ◽  
Tetsuro Minagawa ◽  
Tamami Nonaka ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Light Chain ◽  
Amino Acid Sequences ◽  
Catalytic Antibodies ◽  
Light Chains ◽  
Catalytic Antibody ◽  
Peptidase Activity ◽  
Peptide Substrate ◽  
Catalytic Function ◽  
Conserved Residue

Over thousands of monoclonal antibodies (mAbs) have been produced so far, and it would be valuable if these mAbs could be directly converted into catalytic antibodies. We have designed a system to realize the above concept by deleting Pro95, a highly conserved residue in CDR-3 of the antibody light chain. The deletion of Pro95 is a key contributor to catalytic function of the light chain. The S35 and S38 light chains have identical amino acid sequences except for Pro95. The former, with Pro95 did not show any catalytic activity, whereas the latter, without Pro95, exhibited peptidase activity. To verify the generality of this finding, we tested another light chain, T99wt, which had Pro95 and showed little catalytic activity. In contrast, a Pro95-deleted mutant enzymatically degraded the peptide substrate and amyloid-beta molecule. These two cases demonstrate the potential for a new method of creating catalytic antibodies from the corresponding mAbs.

Catalytic antibody light chain capable of cleaving a chemokine receptor CCR-5 peptide with a high reaction rate constant

2004 ◽  
Vol 86 (2) ◽  
pp. 217-225 ◽  
Author(s):  
Yukie Mitsuda ◽  
Emi Hifumi ◽  
Kumi Tsuruhata ◽  
Hiroko Fujinami ◽  
Naoki Yamamoto ◽  
...  
Keyword(s):  
Rate Constant ◽  
Chemokine Receptor ◽  
Light Chain ◽  
Reaction Rate ◽  
Reaction Rate Constant ◽  
Catalytic Antibody ◽  
High Reaction ◽  
High Reaction Rate

scholarly journals Human Autoantibody Silencing by Immunoglobulin Light Chains

2004 ◽  
Vol 200 (2) ◽  
pp. 191-199 ◽  
Author(s):  
Hedda Wardemann ◽  
Johanna Hammersen ◽  
Michel C. Nussenzweig
Keyword(s):  
Light Chain ◽  
Light Chains ◽  
Receptor Editing ◽  
Immunoglobulin Light Chains ◽  
Human Antibodies ◽  
Normal Individuals ◽  
Isoelectric Points ◽  
Autoreactive Antibody ◽  
Cell Deletion ◽  
Complementarity Determining Region

Several newly arising human antibodies are polyreactive, but in normal individuals the majority of these potentially autodestructive antibodies are removed from the repertoire by receptor editing or B cell deletion in the bone marrow. To determine what proportion of naturally arising autoantibodies can be silenced by immunoglobulin (Ig) light chain receptor editing, we replaced the light chains in 12 such antibodies with a panel of representative Igκ and Igλ chains. We found that most naturally arising autoantibodies are readily silenced by light chain exchange. Thus, receptor editing may account for most autoreactive antibody silencing in humans. Light chain complementarity determining region (CDR) isoelectric points did not correlate with silencing activity, but Igλ genes were more effective than Igκ genes as silencers. The greater efficacy of Igλ chains as silencer of autoreactivity provides a possible explanation for the expansion and altered configuration of the Igλ locus in evolution.

Targeted destruction of the HIV-1 coat protein gp41 by a catalytic antibody light chain

2002 ◽  
Vol 269 (1-2) ◽  
pp. 283-298 ◽  
Author(s):  
Emi Hifumi ◽  
Yukie Mitsuda ◽  
Kyoko Ohara ◽  
Taizo Uda
Keyword(s):  
Coat Protein ◽  
Light Chain ◽  
Catalytic Antibody ◽  
Protein Gp41 ◽  
Hiv 1

Biochemical features and antiviral activity of a monomeric catalytic antibody light‐chain 23D4 against influenza A virus

2015 ◽  
Vol 29 (6) ◽  
pp. 2347-2358 ◽  
Author(s):  
Emi Hifumi ◽  
Mitsue Arakawa ◽  
Shingo Matsumoto ◽  
Tatsuhiro Yamamoto ◽  
Yoshiki Katayama ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Influenza A Virus ◽  
Light Chain ◽  
Influenza A ◽  
Catalytic Antibody ◽  
Biochemical Features
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