ArticleProceedings of the National Academy of Sciences of the United States of America1996
Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 89 citations in OpenAlex.
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- Signal peptide exchange alters HIV-1 envelope antigenicity and immunogenicity.Frontiers in immunology · 2024Article
- Broadly neutralizing antibody epitopes on HIV-1 particles are exposed after virus interaction with host cells.Journal of virology · 2023Article
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- SYNJ2BP Improves the Production of Lentiviral Envelope Protein by Facilitating the Formation of Mitochondrion-Associated Endoplasmic Reticulum Membrane.Journal of virology · 2022Article
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- A slowly cleaved viral signal peptide acts as a protein-integral immune evasion domain.Nature communications · 2021Article
- HIV-1 Envelope Glycosylation and the Signal Peptide.Vaccines · 2021Review
- Signal peptide of HIV-1 envelope modulates glycosylation impacting exposure of V1V2 and other epitopes.PLoS pathogens · 2020Article
- Protein and Glycan Mimicry in HIV Vaccine Design.Journal of molecular biology · 2019Review
- Production of complex viral glycoproteins in plants as vaccine immunogens.Plant biotechnology journal · 2018Review
- Advances in HIV-1 Vaccine Development.Viruses · 2018Review
- Signal peptide of HIV envelope protein impacts glycosylation and antigenicity of gp120.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Alterations of HIV-1 envelope phenotype and antibody-mediated neutralization by signal peptide mutations.PLoS pathogens · 2018Article
- Article
- The roles of direct recognition by animal lectins in antiviral immunity and viral pathogenesis.Molecules (Basel, Switzerland) · 2015Review
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- Protein folding in the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- Identification of a cluster of HIV-1 controllers infected with low replicating viruses.PloS one · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The HIV-1 envelope glycoprotein gp120 displays inefficient intracellular transport, which is caused by its retention in the endoplasmic reticulum. Coexpression in insect cells (Sf9) of HIV-1 gp120 with calnexin has shown that their interaction was modulated by the signal sequence of HIV-1 gp120. gp120, with its natural signal sequence, showed a prolonged association with calnexin with a t1/2 of greater than 20 min. Replacement of the natural signal sequence with the signal sequence from mellitin led to a decreased time of association of gp120 with calnexin (t1/2 < 10 min). These different times of calnexin association coincided both with the folding of gp120 as measured by the ability of bind CD4 and with endoplasmic reticulum to Golgi transport as analyzed by the acquisition of partial endoglycosidase H resistance. Using a monospecific antibody to the HIV-1 gp120 natural signal peptide, we showed that calnexin associated with N-glycosylated but uncleaved gp120. Only after dissociation from calnexin was gp120 cleaved, but very inefficiently. Only the small proportion of signal-cleaved gp120 molecules acquired transport competence and were secreted. This is the first report demonstrating the effect of the signal sequence on calnexin association.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.