Inhibition of Secretion of Hepatitis B Surface Antigen by a Related Presurface Polypeptide
1986; American Association for the Advancement of Science; Volume: 234; Issue: 4782 Linguagem: Inglês
10.1126/science.3787251
ISSN1095-9203
AutoresDavid H. Persing, Harold Varmus, Don Ganem,
Tópico(s)Bacteriophages and microbial interactions
ResumoThe presurface (preS) proteins of hepatitis B virus are structural components of the viral envelope that may play important roles in virion assembly and infectivity. They are specified by a large open reading frame that includes the coding region for the major surface (S) protein in its 3′ half. Translation of the preS proteins initiates upstream from the S region, giving rise to proteins that are composed of the S domain and an additional 163 (preS1) or 55 (preS2) amino acids. Little is known about the biosynthesis and assembly of these proteins. The expression of the S and preS1 proteins was examined by transfecting cultured mammalian cells with viral DNA and injecting synthetic messenger RNA's into Xenopus oocytes. In contrast to the proteins encoded by the S region, the preS1 proteins are not detectably secreted into the culture medium. Furthermore, when the S and preS1 proteins are synthesized together, secretion of the S proteins is specifically and strongly inhibited. The results suggest a unique molecular interaction during secretion of the S and preS proteins that may be important for virus assembly.
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