Abstract
Recombinant polioviruses expressing antigens from rotavirus, herpes simplex virus type 2, and hepatitis B virus were generated. Fusion of the heterologous polypeptides to the amino terminus of the poliovirus polyprotein did not prevent myristylation of VP0, suggesting a novel mechanism of myristylation for these recombinant viruses. The effects of the parental genetic background, different foreign sequences, and different insert sizes on growth characteristics were compared. Both the size and the nature of the heterologous sequence appeared to be factors influencing the growth and stability of recombinant polioviruses. All of the recombinants showed a temperature-sensitive phenotype, regardless of the genetic background (attenuated or wild type) from which they were derived. Preliminary studies with transgenic mice carrying the poliovirus receptor gene are discussed.
Full Text
The Full Text of this article is available as a PDF (298.1 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Andino R., Silvera D., Suggett S. D., Achacoso P. L., Miller C. J., Baltimore D., Feinberg M. B. Engineering poliovirus as a vaccine vector for the expression of diverse antigens. Science. 1994 Sep 2;265(5177):1448–1451. doi: 10.1126/science.8073288. [DOI] [PubMed] [Google Scholar]
- Ansardi D. C., Moldoveanu Z., Porter D. C., Walker D. E., Conry R. M., LoBuglio A. F., McPherson S., Morrow C. D. Characterization of poliovirus replicons encoding carcinoembryonic antigen. Cancer Res. 1994 Dec 15;54(24):6359–6364. [PubMed] [Google Scholar]
- Ansardi D. C., Porter D. C., Morrow C. D. Myristylation of poliovirus capsid precursor P1 is required for assembly of subviral particles. J Virol. 1992 Jul;66(7):4556–4563. doi: 10.1128/jvi.66.7.4556-4563.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chow M., Newman J. F., Filman D., Hogle J. M., Rowlands D. J., Brown F. Myristylation of picornavirus capsid protein VP4 and its structural significance. Nature. 1987 Jun 11;327(6122):482–486. doi: 10.1038/327482a0. [DOI] [PubMed] [Google Scholar]
- Isola V. J., Eisenberg R. J., Siebert G. R., Heilman C. J., Wilcox W. C., Cohen G. H. Fine mapping of antigenic site II of herpes simplex virus glycoprotein D. J Virol. 1989 May;63(5):2325–2334. doi: 10.1128/jvi.63.5.2325-2334.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kitamura N., Semler B. L., Rothberg P. G., Larsen G. R., Adler C. J., Dorner A. J., Emini E. A., Hanecak R., Lee J. J., van der Werf S. Primary structure, gene organization and polypeptide expression of poliovirus RNA. Nature. 1981 Jun 18;291(5816):547–553. doi: 10.1038/291547a0. [DOI] [PubMed] [Google Scholar]
- Landolfi V., Zarley C. D., Abramovitz A. S., Figueroa N., Wu S. L., Blasiak M., Ishizaka S. T., Mishkin E. M. Baculovirus-expressed herpes simplex virus type 2 glycoprotein D is immunogenic and protective against lethal HSV challenge. Vaccine. 1993;11(4):407–414. doi: 10.1016/0264-410x(93)90280-b. [DOI] [PubMed] [Google Scholar]
- Larralde G., Gorziglia M. Distribution of conserved and specific epitopes on the VP8 subunit of rotavirus VP4. J Virol. 1992 Dec;66(12):7438–7443. doi: 10.1128/jvi.66.12.7438-7443.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Larralde G., Li B. G., Kapikian A. Z., Gorziglia M. Serotype-specific epitope(s) present on the VP8 subunit of rotavirus VP4 protein. J Virol. 1991 Jun;65(6):3213–3218. doi: 10.1128/jvi.65.6.3213-3218.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- López S., Arias C. F., Bell J. R., Strauss J. H., Espejo R. T. Primary structure of the cleavage site associated with trypsin enhancement of rotavirus SA11 infectivity. Virology. 1985 Jul 15;144(1):11–19. doi: 10.1016/0042-6822(85)90300-9. [DOI] [PubMed] [Google Scholar]
- Macadam A. J., Ferguson G., Burlison J., Stone D., Skuce R., Almond J. W., Minor P. D. Correlation of RNA secondary structure and attenuation of Sabin vaccine strains of poliovirus in tissue culture. Virology. 1992 Aug;189(2):415–422. doi: 10.1016/0042-6822(92)90565-7. [DOI] [PubMed] [Google Scholar]
- Mackow E. R., Shaw R. D., Matsui S. M., Vo P. T., Dang M. N., Greenberg H. B. The rhesus rotavirus gene encoding protein VP3: location of amino acids involved in homologous and heterologous rotavirus neutralization and identification of a putative fusion region. Proc Natl Acad Sci U S A. 1988 Feb;85(3):645–649. doi: 10.1073/pnas.85.3.645. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mattion N. M., Mitchell D. B., Both G. W., Estes M. K. Expression of rotavirus proteins encoded by alternative open reading frames of genome segment 11. Virology. 1991 Mar;181(1):295–304. doi: 10.1016/0042-6822(91)90495-w. [DOI] [PubMed] [Google Scholar]
- Mattion N. M., Reilly P. A., DiMichele S. J., Crowley J. C., Weeks-Levy C. Attenuated poliovirus strain as a live vector: expression of regions of rotavirus outer capsid protein VP7 by using recombinant Sabin 3 viruses. J Virol. 1994 Jun;68(6):3925–3933. doi: 10.1128/jvi.68.6.3925-3933.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Milich D. R., Thornton G. B., Neurath A. R., Kent S. B., Michel M. L., Tiollais P., Chisari F. V. Enhanced immunogenicity of the pre-S region of hepatitis B surface antigen. Science. 1985 Jun 7;228(4704):1195–1199. doi: 10.1126/science.2408336. [DOI] [PubMed] [Google Scholar]
- Ogra P. L. Mucosal immune response to poliovirus vaccines in childhood. Rev Infect Dis. 1984 May-Jun;6 (Suppl 2):S361–S368. doi: 10.1093/clinids/6.supplement_2.s361. [DOI] [PubMed] [Google Scholar]
- Pallai P. V., Burkhardt F., Skoog M., Schreiner K., Bax P., Cohen K. A., Hansen G., Palladino D. E., Harris K. S., Nicklin M. J. Cleavage of synthetic peptides by purified poliovirus 3C proteinase. J Biol Chem. 1989 Jun 15;264(17):9738–9741. [PubMed] [Google Scholar]
- Palmenberg A. C. Proteolytic processing of picornaviral polyprotein. Annu Rev Microbiol. 1990;44:603–623. doi: 10.1146/annurev.mi.44.100190.003131. [DOI] [PubMed] [Google Scholar]
- Prasad B. V., Burns J. W., Marietta E., Estes M. K., Chiu W. Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy. Nature. 1990 Feb 1;343(6257):476–479. doi: 10.1038/343476a0. [DOI] [PubMed] [Google Scholar]
- Ren R. B., Costantini F., Gorgacz E. J., Lee J. J., Racaniello V. R. Transgenic mice expressing a human poliovirus receptor: a new model for poliomyelitis. Cell. 1990 Oct 19;63(2):353–362. doi: 10.1016/0092-8674(90)90168-e. [DOI] [PubMed] [Google Scholar]
- Ren R., Racaniello V. R. Human poliovirus receptor gene expression and poliovirus tissue tropism in transgenic mice. J Virol. 1992 Jan;66(1):296–304. doi: 10.1128/jvi.66.1.296-304.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stanway G., Hughes P. J., Mountford R. C., Reeve P., Minor P. D., Schild G. C., Almond J. W. Comparison of the complete nucleotide sequences of the genomes of the neurovirulent poliovirus P3/Leon/37 and its attenuated Sabin vaccine derivative P3/Leon 12a1b. Proc Natl Acad Sci U S A. 1984 Mar;81(5):1539–1543. doi: 10.1073/pnas.81.5.1539. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Taniguchi K., Maloy W. L., Nishikawa K., Green K. Y., Hoshino Y., Urasawa S., Kapikian A. Z., Chanock R. M., Gorziglia M. Identification of cross-reactive and serotype 2-specific neutralization epitopes on VP3 of human rotavirus. J Virol. 1988 Jul;62(7):2421–2426. doi: 10.1128/jvi.62.7.2421-2426.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tatem J. M., Weeks-Levy C., Georgiu A., DiMichele S. J., Gorgacz E. J., Racaniello V. R., Cano F. R., Mento S. J. A mutation present in the amino terminus of Sabin 3 poliovirus VP1 protein is attenuating. J Virol. 1992 May;66(5):3194–3197. doi: 10.1128/jvi.66.5.3194-3197.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weeks-Levy C., Tatem J. M., DiMichele S. J., Waterfield W., Georgiu A. F., Mento S. J. Identification and characterization of a new base substitution in the vaccine strain of Sabin 3 poliovirus. Virology. 1991 Dec;185(2):934–937. doi: 10.1016/0042-6822(91)90576-w. [DOI] [PubMed] [Google Scholar]
- Ypma-Wong M. F., Dewalt P. G., Johnson V. H., Lamb J. G., Semler B. L. Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor. Virology. 1988 Sep;166(1):265–270. doi: 10.1016/0042-6822(88)90172-9. [DOI] [PubMed] [Google Scholar]
- van der Werf S., Bradley J., Wimmer E., Studier F. W., Dunn J. J. Synthesis of infectious poliovirus RNA by purified T7 RNA polymerase. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2330–2334. doi: 10.1073/pnas.83.8.2330. [DOI] [PMC free article] [PubMed] [Google Scholar]