Cloning of a hamster anti-mouse CD79B antibody sequences and identification of a new hamster immunoglobulin lambda constant IGLC gene region

Haggart, Ryan; Perera, Jason; Huang, Haochu

doi:10.1007/s00251-013-0698-5

Cited by 1 publication

(1 citation statement)

References 27 publications

(34 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To rule out the possibilities that the observed effects were specific for mouse hybridoma-derived antibodies or for the recognized mCD39 antigen only, we used WT and Fut8 −/− CHO cells to recombinantly express an Armenian hamster ( Cricetulus migratorius ) anti-mouse CD79b antibody (clone HM79-16 or HM79b; [ 37 ]). The original HM79–16 hamster antibody has IgG2 heavy chain (GenBank: AGH06135 ) and lambda light chain (GenBank: AGH06134 ).…”

Section: Methodsmentioning

confidence: 99%

Cross-species higher sensitivities of FcγRIIIA/FcγRIV to afucosylated IgG for enhanced ADCC

Mao

Near

Zhong

et al. 2021

Antibody Therapeutics

View full text Add to dashboard Cite

Background Expressing afucosylated human IgG1 antibodies with Chinese hamster ovary (CHO) cells deficient of α-(1,6)-fucosyltransferase (FUT8) is being more and more accepted as a routine method to enhance antibody-dependent cellular cytotoxicity (ADCC) of therapeutic antibodies, especially for anti-cancer regimens. However, in pre-clinical studies relying on disease models other than mice and primates, e.g., those underrepresented species for infectious diseases, it is less clear whether such afucosylated antibodies can demonstrate enhanced therapeutic index. This is because the orthologues of human FcγRIIIA or mouse FcγRIV from those species have not been well characterized. Methods We set up a luciferase-based ADCC assay with Jurkat reporter cells expressing FcγRIIIA/FcγRIV from human, mouse, rat, hamster, guinea pig, ferret, rabbit, cat, dog, pig and monkey, and also produced human, mouse, hamster, rabbit and pig IgG from wild type and Fut8−/− CHO cells or hybridomas. Results We confirmed that enhanced stimulation through FcγRIIIA/FcγRIV by afucosylated IgG, as compared with wild type IgG, is a cross-species phenomenon. Conclusions Thus, efficacy and toxicology studies of the next generation afucosylated therapeutic IgG and Fc fusion proteins in these underrepresented animal models should be expected to generate translatable data for treating human diseases, leading to the expanded applications of this new class of glycoengineered biologics.

show abstract

Section: Methodsmentioning

confidence: 99%