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Antibodies to the Epstein-Barr virus transactivator protein (ZEBRA) as a valuable biomarker in young patients with nasopharyngeal carcinoma

✍ Scribed by R'kia Dardari; Meriem Khyatti; Abdellatif Benider; Hassan Jouhadi; Abdelouahad Kahlain; Chantal Cochet; Aziz Mansouri; Brahim El Gueddari; Abdellah Benslimane; Irène Joab


Publisher
John Wiley and Sons
Year
2000
Tongue
French
Weight
54 KB
Volume
86
Category
Article
ISSN
0020-7136

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✦ Synopsis


Epstein-Barr virus (EBV)-associated nasopharyngeal carcinoma (NPC) generally occurs in adults, especially in high-prevalence populations such as the Chinese and Eskimos. In Maghrebian populations, young patients affected with this malignancy represent 25% of the total NPC cases. In adults with NPC, relatively high titers of IgA antibodies to the EBV viral capsid antigen (VCA) and early antigen (EA) represent important markers. However, nearly 50% of young NPC patients are negative for IgA-anti-VCA and -EA or exhibit very low titers of these antibodies. We report here that 92% of sera from young NPC patients negative for IgA-EA and 89% of those negative for IgA-VCA were positive for IgG antibodies to the EBV transactivator protein (ZEBRA) at very high titers. Our results show that in young patients with NPC these antibodies represent the most reliable marker for diagnosis and prognosis, particularly when compared with conventional NPC markers, i.e., IgA-VCA (58%) and anti-EA (25%). The titers of IgG-ZEBRA antibodies increased along with lymph node involvement only in the young patient group, suggesting a prognostic value of this marker in this patient group.


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Antibody against the Epstein-Barr virus
✍ Liu, Mei-Ying; Shih, Ya-Yi; Chou, Sheng-Ping; Chen, Chien-Jen; Sheen, Tzung-Shia 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 269 KB 👁 1 views

The Epstein-Barr virus (EBV) open reading frame BHRF1, a homologue of the oncogene bcl-2, was cloned from a patient with nasopharyngeal carcinoma (NPC) and overexpressed in Escherichia coli. The resulting recombinant BHRF1 fusion protein, with an apparent molecular weight of 35 KD, was used as antig