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• W2030481100 abstract "Muc1-H23 is a cell surface mucin that is expressed on normal breast luminal epithelial cells and over-expressed in most breast tumors. In addition, Muc-1 expressed by malignant cells is glycosylated differently than Muc-1 expressed by normal cells. This difference in glycosylation exposes a peptide epitope on malignant cells which is not exposed on normal cells. Murine monoclonal antibody H23 recognizes this epitope and stains 91% of breast cancers, but only 1/56 non-malignant breast tissue samples.To create a human antibody that was equivalent to H23 for potential uses in imaging and/or the therapy of breast cancer.We decided to humanize H23 by CDR-grafting using overlap PCR, and to this end, designed and constructed a bacterial expression vector that would allow V-regions, cloned via unique restriction sites, to be expressed as Fab fragments. In this way, we hoped to be able to rapidly evaluate Fab constructs for binding to Muc-1 and to cells and tissue sections that expressed the antigen.A fully humanized Fab fragment was able to bind Muc-1 peptide, as well as breast cancer cells known to express the epitope and tissue sections, generally showing the same reactivity as the native antibody. In addition, an analysis of sFab expressed with a [His]6 tag preceded by a factor Xa proteolytic cleavage site suggested that E. coli periplasmic signal peptidase was able to cleave the factor Xa site, thereby removing the [His]6 tag.We have generated a human antibody that is capable of recognizing a tumor specific epitope expressed by 91% of breast cancers." @default.
• W2030481100 created "2016-06-24" @default.
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• W2030481100 date "1997-03-01" @default.
• W2030481100 modified "2023-10-18" @default.
• W2030481100 title "Humanization of an antibody recognizing a breast cancer specific epitope by CDR-grafting" @default.
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• W2030481100 doi "https://doi.org/10.1016/s1380-2933(96)00063-2" @default.
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