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. 1979 Dec;32(3):710–716. doi: 10.1128/jvi.32.3.710-716.1979

Immunochemical Characterization of Epstein-Barr Virus-Associated Early and Late Antigens in n-Butyrate-Treated P3HR-1 Cells

Bengt Kallin 1, Janos Luka 1, George Klein 1
PMCID: PMC525917  PMID: 229261

Abstract

Sodium butyrate induces the Epstein-Barr virus cycle in latently infected P3HR-1 cells with a high efficiency. This fact was utilized for the metabolic labeling of the Epstein-Barr virus antigens. Nonproducer Raji cells, lacking both early antigen and viral capsid antigen, were used as controls. Immunoprecipitation patterns were compared with 13 anti-Epstein-Barr virus (viral capsid antigen) - positive and 3 negative sera. Sixteen polypeptides were identified as being associated with the lytic Epstein-Barr virus cycle. Their molecular weights ranged from 31,000 (31K) to 275K on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two polypeptides, 158K and 165K, could be classified as late viral products on the basis of their sensitivity to cytosine arabinoside. Six of the polypeptides, i.e., 90K, 95K, 134K, 165K, 236K, and 275K, were detected by [3H]glucosamine labeling. Among the early, cytosine arabinoside-insensitive polypeptides detected by [35S]methionine labeling, a 152K component appears to be a major constituent of early antigen. This polypeptide was precipitated by all anti-Epstein-Barr virus-positive sera tested. As a rule, together with the 103K and 134K polypeptides, the 152K component is precipitated by anti-early antigen, R (restricted) antibodies. In addition, anti-early antigen D (diffuse) antibodies precipitate 31K, 51K, 65K, and 90K components.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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