ArticleProceedings of the National Academy of Sciences of the United States of America1992
Chimeric gag-V3 virus-like particles of human immunodeficiency virus induce virus-neutralizing antibodies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 50 citations in OpenAlex.
- Enterovirus 71 vaccine: close but still far.International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2010Review
- Biological gene delivery vehicles: beyond viral vectors.Molecular therapy : the journal of the American Society of Gene Therapy · 2009Review
- Expression, purification and characterization of enterovirus-71 virus-like particles.World journal of gastroenterology · 2006Article
- Vaccines for viral and parasitic diseases produced with baculovirus vectors.Advances in virus research · 2006Review
- Production of a recombinant major inner capsid protein for serological detection of epizootic hemorrhagic disease virus.Clinical and diagnostic laboratory immunology · 2005Article
- Baculovirus as a highly efficient expression vector in insect and mammalian cells.Acta pharmacologica Sinica · 2005Review
- HIV type 1 Gag virus-like particle budding from spheroplasts of Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Location, exposure, and conservation of neutralizing and nonneutralizing epitopes on human immunodeficiency virus type 2 SU glycoprotein.Journal of virology · 1996Article
- Flow cytometric immunofluorescence assay for detection of antibodies to human immunodeficiency virus type 1 using insoluble precursor forms of recombinant polyproteins as carriers and antigens.Journal of clinical microbiology · 1996Article
- Release of virus-like particles from cells infected with poliovirus replicons which express human immunodeficiency virus type 1 Gag.Journal of virology · 1996Article
- Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus.Journal of virology · 1993Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A 41-kDa unprocessed human immunodeficiency virus 2 (HIV-2) gag precursor protein that has a deletion of a portion of the viral protease assembles as virus-like particles by budding through the cytoplasmic membrane of recombinant baculovirus-infected insect cells. We have constructed six different combinations of chimeric genes by coupling the truncated HIV-2 gag gene to the neutralizing domain (V3) or the neutralizing and the CD4 binding domains (V3+CD4BD) of gp120 env gene sequences from HIV-1 or HIV-2. The env gene sequences were inserted either into the middle of the gag gene or at the 3' terminus of the gag gene. Virus-like particles were formed by chimeric gene products only when the env gene sequences were linked to the 3' terminus of the gag gene. Insertion of env gene sequence in the middle of the gag gene resulted in high-level chimeric gene expression but without the formation of virus-like particles. Three different chimeric genes [gag gene with HIV-1 V3 (1V3), gag gene with HIV-2 V3 (2V3), and gag gene with HIV-2 V3+CD4BD (2V3+CD4BD)] formed virus-like particles that were secreted into the cell culture medium. In contrast, the HIV-1 V3+CD4BD/HIV-2 gag construct did not form virus-like particles. The chimeric gag-env particles had spherical morphology and the size was slightly larger than that of the gag particles, but the chimeric particles were similar to the mature HIV particles. Western blot analysis showed that the gag-env chimeric proteins were recognized by antibodies in HIV-positive human serum and rabbit anti-gp120 serum. Rabbit anti-gag 1V3 and anti-gag 2V3 sera reacted with authentic gp120 of HIV-1 and HIV-2, respectively, and neutralized homologous HIV infectivity. Our results show that precursor gag protein has potential as a carrier for the presentation of foreign epitopes in good immunological context. The gag protein is highly immunogenic and has the ability to carry large foreign inserts; as such, it offers an attractive approach for HIV vaccine development.
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