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Generation of monoclonal antibodies against Hong Kong nasopharyngeal carcinoma-associated Epstein-Barr virus latent membrane protein 1 (LMP1). | LitMetric

AI Article Synopsis

  • - A set of monoclonal antibodies has been created that specifically targets variants of the Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) linked to nasopharyngeal carcinoma (NPC) in Hong Kong Chinese populations!* - These antibodies can distinguish between local LMP1 variants and the prototype found in Caucasian infectious mononucleosis, as well as two deletion variants common in Hong Kong NPC.* - The predominant variant, DV-Asp335, has an aspartic acid at residue 335, while another minor variant, DV-Gly335, has a glycine, and these antibodies could help study the role of the 335D variant in NPC.*

Article Abstract

A panel of monoclonal antibodies specific to Hong Kong Chinese nasopharyngeal carcinoma (NPC)-associated Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) variants has been generated. These monoclonal antibodies not only differentiate the Hong Kong Chinese NPC-associated LMP1 variants from the prototype B95-8 LMP1, derived from Caucasian infectious mononucleosis, but also differentiate the 2 highly homologous LMP1 deletion variants commonly found in Hong Kong primary NPC. The predominant deletion type variant, DV-Asp335, is characterized by an aspartic acid at residue 335 located in the cytoplasmic C-terminal region, whereas the other minor deletion variant, DV-Gly335, has a glycine in the same residue position. 335D is hitherto found predominantly in LMP1 of the China 1 strain in association with NPC in the Chinese populations located in southern China and Malaysia. These antibodies, which are applicable in ELISA, immunofluorescence, immunoprecipitation, immunoblotting and immunohistochemistry on paraffin sections, are the first variant-specific anti-LMP1 monoclonal antibodies produced, and will be useful in investigating the functional significance of 335D in NPC.

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Source
http://dx.doi.org/10.1002/ijc.10773DOI Listing

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