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CD176 single-chain variable antibody fragment inhibits the adhesion of cancer cells to endothelial cells and hepatocytes

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Frontiers of Medicine 2016年第2期10卷 204-211页

作者： Jiangnan Liu Bin Yi Zhe Zhang Yi Cao Laboratory of Molecular and Experimental Pathology Kunming Institute of Zoology Chinese Academy of Sciences Kunming 650223 China Kunming College of Life Science University of Chinese Academy of Sciences Kunming 650223 China

CD176 （thomsen-friedenreich antigen） is a tumor-associated carbohydrate epitope （glycotope） functionally involved in blood spread and fiver metastasis of cancer cells by mediating the adhesion of cancer cells to endothelial cells and hepatocytes, respectively. CD176 could be a promising target for antitumor immunotherapy. We applied B lymphocytes obtained from mice immunized with CD176 antigen and constructed a phage display library. A positive clone of CD176 single-chain variable antibody fragment （scFv） was successfully screened from this library. The CD176 scFv was expressed in Escherichia coli and purified. The purified scFv can bind to the natural CD176 expressed on the surface of cancer cells. Furthermore, the CD176 scFv inhibits the adhesion of CD176＋ cancer cells to endothelial cells and hepatocytes. This CD176 scFv provides a basis for future development of recombinant CD176-specific antibodies that can be used in therapeutic application.

关键词： CD 176 thomsen-friedenreich antigen scFv cancer therapy adhesion metastasis

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Preterminal protein,the achilles heel of adenoviridae:Implications for adenoviral infections

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World Journal of Pharmacology 2024年第2期13卷 1-9页

作者： Harold A Walsh Faculty of Pharmacy Division of PharmacologyRhodes UniversityGrahamstown 6139Eastern CapeSouth Africa

Adenoviruses pose a serious health risk particularly in the absence of any clinically approved *** adenoviral infections are quite frequent and recent outbreaks manifest more virulent variant strains,the need to develop an effective treatment remains a *** adenoviral protein,preterminal protein(pTP),is one of the key common products of the viral lifecycle as it is necessary to initiate viral replication and hence the infection *** makes pTP a potential chemotherapeutic target in the search for and development of an effective treatment for adenoviral induced *** we report,for the first time,that glycosylation of pTP in situ prevents binding to ssDNA in *** To explore whether specific structural tailoring of the adenoviral protein pTP,imparts the potential to scupper the viral replication *** All chemicals used were of reagent *** of pTP was achieved using the‘BAC to BAC’expression *** presence and relative concentration of the protein was determined throughout the incubation period by the Bradford *** pTP was identified by MALDI-TOFF and sodium dodecyl sulphate polyacrylamide gel *** the removal of the aminosugar,a deglycosylase enzyme kit from PROZYME was *** of cloned pTP(6xHis)was done with a ssDNA cellulose column followed by a Ni-NTA ***-tags were excised with the Tobacco etch virus *** fractionation was performed with a fraction collector coupled to a UV detector(280 nm)from *** The pTP overexpressed in insect cells(Spodoptera frugiperda)(>96 hours),is unable to bind to ssDNA in *** of this unbound protein with a deglycosidase enzyme that is specific for the removal of truncated unsubstituted O-linked Galβ(1-3)GalNAc-α1 disaccharides bound to Thr or Ser in a glycoprotein,restores binding to *** is presented as a linegraph for both the glycosylated and the deglycosylated *** point repr

关键词： thomsen-friedenreich antigen Adenoviral Preterminal protein Spodoptera frugiperda cells Protein priming mechanism Glycosylation

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