Generation of a chickenized catalytic anti-nucleic acid antibody by complementarity-determining region grafting

Roh, Jooho; Byun, Sung June; Seo, Youngsil; Kim, Minjae; Lee, Jae-Ho; Kim, Songmi; Lee, Yuno; Lee, Keun Woo; Kim, Jin‐Kyoo; Kwon, Myung-Hee

doi:10.1016/j.molimm.2014.10.009

Cited by 6 publications

(5 citation statements)

References 44 publications

(44 reference statements)

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“…This compatibility of V-C region interfaces between mouse and chicken Abs is supported by a report showing that chimeric chicken-human Abs composed of chicken V domains and human C domains exhibit similar binding affinity to parental chicken Abs 37 . Furthermore, V-C region compatibility between these species has been observed in a chickenized single-chain variable fragment (scFv) Ab harboring complementarity-determining regions (CDRs) of the mouse Ab and framework regions (FRs) of a chicken Ab 38 .…”

Section: Discussionmentioning

confidence: 99%

Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains

Choi

Kim

Lee

et al. 2019

Sci Rep

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Constant (C)-region switching of heavy (H) and/or light (L) chains in antibodies (Abs) can affect their affinity and specificity, as demonstrated using mouse, human, and chimeric mouse-human (MH) Abs. However, the consequences of C-region switching between evolutionarily distinct mammalian and avian Abs remain unknown. To explore C-region switching in mouse-chicken (MC) Abs, we investigated antigen-binding parameters and thermal stability of chimeric MC-6C407 and MC-3D8 IgY Abs compared with parental mouse IgGs and chimeric MH Abs (MH-6C407 IgG and MH-3D8 IgG) bearing identical corresponding variable (V) regions. The two MC-IgYs exhibited differences in antigen-binding parameters and thermal stability from their parental mouse Abs. However, changes were similar to or less than those between chimeric MH Abs and their parental mouse Abs. The results demonstrate that mammalian and avian Abs share compatible V-C region interfaces, which may be conducive for the design and utilization of mammalian-avian chimeric Abs.

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Section: Discussionmentioning

confidence: 99%

Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains

Choi

Kim

Lee

et al. 2019

Sci Rep

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“…As the most variable parts of the molecules, CDRs are crucial to the diversity of antigen specificities. Within the variable domain, CDR I, CDR II, and CDR III are found in the variable region of a polypeptide chain, and CDRIII is the most variable [18], [19], [20], [33], [34].…”

Section: Resultsmentioning

confidence: 99%

Construction and sequencing analysis of scFv antibody fragment derived from monoclonal antibody against norfloxacin (Nor155)

Mala

Puthong

Maekawa

et al. 2017

Journal of Genetic Engineering and Biotechnology

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Norfloxacin belongs to the group of fluoroquinolone antibiotics which has been approved for treatment in animals. However, its residues in animal products can pose adverse side effects to consumer. Therefore, detection of the residue in different food matrices must be concerned. In this study, a single chain variable fragment (scFv) that recognizes norfloxacin antibiotic was constructed. The cDNA was synthesized from total RNA of hybridoma cells against norfloxacin. Genes encoding VH and VL regions of monoclonal antibody against norfloxacin (Nor155) were amplified and size of VH and VL fragments was 402 bp and 363 bp, respectively. The scFv of Nor155 was constructed by an addition of (Gly4Ser)3 as a linker between VH and VL regions and subcloned into pPICZαA, an expression vector of Pichia pastoris. The sequence of scFv Nor155 (GenBank No. AJG06891.1) was confirmed by sequencing analysis. The complementarity determining regions (CDR) I, II, and III of VH and VL were specified by Kabat method. The obtained recombinant plasmid will be useful for production of scFv antibody against norfloxacin in P. pastoris and further engineer scFv antibody against fluoroquinolone antibiotics.

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“…Chickenized antibodies can be generated by fusion with the Fc of chicken IgY and CDR grafting. Although chickenized antibodies with CDR grafting were proven to have reduced immunogenicity in chickens, it is difficult to generate similar variable region structures because of conserved framework regions (FRs) in chicken IgY (Lee et al 2017 ; Roh et al 2015 ). The Fab gene of mouse-derived mAb 1G8 was fused with the chicken Fc gene and expressed in a secretory form in COS-1 cells.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, breakthroughs in antibody phage display and monoclonal antibody (mAb) development have contributed to the development of humanized antiviral antibodies for passive immunization (Chen et al 2017 ; Dong et al 2013 ; Rudraraju and Subbarao 2018 ). However, few antibodies were chickenized for passive immunization of chickens (Roh et al 2015 ). We previously reported a mouse-derived mAb 1G8, that has a significant inhibitory effect on the NA enzyme activity of H9N2 AIV (Wan et al 2016 ).…”

Section: Introductionmentioning

confidence: 99%

Generation of a recombinant chickenized monoclonal antibody against the neuraminidase of H9N2 avian influenza virus

Wang

Wan

et al. 2020

AMB Expr

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We previously reported a monoclonal antibody (mAb), 1G8, against the neuraminidase (NA) of H9N2 avian influenza virus (AIV) with significant NA inhibitory activity. To generate a recombinant chickenized mAb (RCmAb) against the NA of H9N2 AIV for passive immunization in poultry, the gene of the fragment of antigen binding (Fab) of mAb 1G8 was cloned and fused with the fragment crystallizable (Fc) gene of chicken IgY. The RCmAb 1G8 was expressed in COS-1 cells and could be detected in cell culture supernatant. The results of NA inhibitory activity tests of the RCmAb 1G8 in an enzyme-linked lectin assay (ELLA) and a microneutralization (MN) assay showed that the RCmAb 1G8 maintained significant NA inhibitory activity and neutralizing ability. This is the first chickenized antibody against AIV, which would be a good candidate for passive immunization in poultry.

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Generation of a chickenized catalytic anti-nucleic acid antibody by complementarity-determining region grafting

Cited by 6 publications

References 44 publications

Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains

Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains

Construction and sequencing analysis of scFv antibody fragment derived from monoclonal antibody against norfloxacin (Nor155)

Generation of a recombinant chickenized monoclonal antibody against the neuraminidase of H9N2 avian influenza virus

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