Assembly of viral particles in Xenopus oocytes: pre-surface-antigens regulate secretion of the hepatitis B viral surface envelope particle - PubMed (original) (raw)
Assembly of viral particles in Xenopus oocytes: pre-surface-antigens regulate secretion of the hepatitis B viral surface envelope particle
D N Standring et al. Proc Natl Acad Sci U S A. 1986 Dec.
Abstract
Infection with hepatitis B virus (HBV) is associated with the production of a viral envelope particle that contains membrane lipids, surface antigen (S), and two presurface-antigens (pre-S) comprised of the entire S moiety with approximately 55 (pre-S2) and 174 (pre-S1) additional NH2-terminal amino acids. We show here that Xenopus oocytes injected with synthetic S mRNA assemble and secrete characteristic 22-nm viral envelope particles. In contrast, pre-S1 and pre-S2 antigens are synthesized but not secreted. By coinjecting mRNAs, we found that synthesis of high levels of pre-S proteins specifically inhibits S antigen secretion. On the other hand, high levels of S synthesis can drive the secretion of small amounts of either pre-S antigen. These observations are consistent with a model for viral envelope assembly in which both S and pre-S proteins are incorporated into a multimeric particle, presumably via interactions between the S protein domains, while the pre-S amino-terminal moieties regulate the secretion of this structure. Our results indicate that Xenopus oocytes will provide a powerful system for studying the morphogenesis of simple structures of viral or cellular origin.
Similar articles
- Mapping a region of the large envelope protein required for hepatitis B virion maturation.
Bruss V, Thomssen R. Bruss V, et al. J Virol. 1994 Mar;68(3):1643-50. doi: 10.1128/JVI.68.3.1643-1650.1994. J Virol. 1994. PMID: 8107225 Free PMC article. - Infectivity determinants of the hepatitis B virus pre-S domain are confined to the N-terminal 75 amino acid residues.
Blanchet M, Sureau C. Blanchet M, et al. J Virol. 2007 Jun;81(11):5841-9. doi: 10.1128/JVI.00096-07. Epub 2007 Mar 21. J Virol. 2007. PMID: 17376925 Free PMC article. - Immunoadhesins containing pre-S domains of hepatitis B virus large envelope protein are secreted and inhibit virus infection.
Chai N, Gudima S, Chang J, Taylor J. Chai N, et al. J Virol. 2007 May;81(10):4912-8. doi: 10.1128/JVI.02865-06. Epub 2007 Feb 28. J Virol. 2007. PMID: 17329331 Free PMC article. - Functions of the large hepatitis B virus surface protein in viral particle morphogenesis.
Bruss V, Gerhardt E, Vieluf K, Wunderlich G. Bruss V, et al. Intervirology. 1996;39(1-2):23-31. doi: 10.1159/000150471. Intervirology. 1996. PMID: 8957666 Review. - [PreS antigen].
Ishikawa T. Ishikawa T. Nihon Rinsho. 2004 Aug;62 Suppl 8:134-8. Nihon Rinsho. 2004. PMID: 15453302 Review. Japanese. No abstract available.
Cited by
- Three envelope proteins of hepatitis B virus: large S, middle S, and major S proteins needed for the formation of Dane particles.
Ueda K, Tsurimoto T, Matsubara K. Ueda K, et al. J Virol. 1991 Jul;65(7):3521-9. doi: 10.1128/JVI.65.7.3521-3529.1991. J Virol. 1991. PMID: 2041079 Free PMC article. - Hepatitis B virus p25 precore protein accumulates in Xenopus oocytes as an untranslocated phosphoprotein with an uncleaved signal peptide.
Yang SQ, Walter M, Standring DN. Yang SQ, et al. J Virol. 1992 Jan;66(1):37-45. doi: 10.1128/JVI.66.1.37-45.1992. J Virol. 1992. PMID: 1727493 Free PMC article. - Pre- and Post-Transcriptional Control of HBV Gene Expression: The Road Traveled towards the New Paradigm of HBx, Its Isoforms, and Their Diverse Functions.
Villanueva RA, Loyola A. Villanueva RA, et al. Biomedicines. 2023 Jun 9;11(6):1674. doi: 10.3390/biomedicines11061674. Biomedicines. 2023. PMID: 37371770 Free PMC article. Review. - Identification of a promoter region for 3.6-kilobase mRNA of hepatitis B virus and specific cellular binding protein.
Yaginuma K, Koike K. Yaginuma K, et al. J Virol. 1989 Jul;63(7):2914-20. doi: 10.1128/JVI.63.7.2914-2920.1989. J Virol. 1989. PMID: 2542603 Free PMC article. - Novel N-terminal amino acid sequence required for retention of a hepatitis B virus glycoprotein in the endoplasmic reticulum.
Kuroki K, Russnak R, Ganem D. Kuroki K, et al. Mol Cell Biol. 1989 Oct;9(10):4459-66. doi: 10.1128/mcb.9.10.4459-4466.1989. Mol Cell Biol. 1989. PMID: 2586518 Free PMC article.
References
- J Virol. 1983 Oct;48(1):271-80 - PubMed
- Gastroenterology. 1983 Aug;85(2):268-74 - PubMed
- Mol Cell Biol. 1983 Oct;3(10):1766-73 - PubMed
- Methods Enzymol. 1983;96:111-20 - PubMed
- Proc Natl Acad Sci U S A. 1984 Jan;81(1):193-7 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources