ReviewImmunological reviews2012
Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA.
Review in Immunological reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
67 citing papers in PubMed, 92 citations in OpenAlex.
- Safety, pharmacokinetics and neutralization of the broadly neutralizing HIV-1 human monoclonal antibody VRC01 in healthy adults.Clinical and experimental immunology · 2015Trial
- Better neutralization of herpes simplex virus type 1 (HSV-1) than HSV-2 by antibody from recipients of GlaxoSmithKline HSV-2 glycoprotein D2 subunit vaccine.The Journal of infectious diseases · 2014Trial
- Article
- Immunogenicity of differentially glycosylated Marburg virus glycoproteins expressed in mammalian and insect cells.Virology journal · 2025Article
- Article
- Influenza chimeric hemagglutinin structures in complex with broadly protective antibodies to the stem and trimer interface.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Peptides for Vaccine Development.ACS applied bio materials · 2022Review
- RCSB Protein Data Bank resources for structure-facilitated design of mRNA vaccines for existing and emerging viral pathogens.Structure (London, England : 1993) · 2022Article
- Article
- Review
- Peptide-Based Vaccines: Current Progress and Future Challenges.Chemical reviews · 2020Review
- Mannosylated hemagglutinin peptides bind cyanovirin-N independent of disulfide-bonds in complementary binding sites.RSC advances · 2020Article
- Virus-Host Interactions Between Nonsecretors and Human Norovirus.Cellular and molecular gastroenterology and hepatology · 2020Article
- Star nanoparticles delivering HIV-1 peptide minimal immunogens elicit near-native envelope antibody responses in nonhuman primates.PLoS biology · 2019Article
- A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface.Cell · 2019Article
- Antibody responses to viral infections: a structural perspective across three different enveloped viruses.Nature microbiology · 2019Review
- Immunodominance and Antigenic Variation of Influenza Virus Hemagglutinin: Implications for Design of Universal Vaccine Immunogens.The Journal of infectious diseases · 2019Article
- Antigenicity and Immunogenicity of Differentially Glycosylated Hepatitis C Virus E2 Envelope Proteins Expressed in Mammalian and Insect Cells.Journal of virology · 2019Article
- VCurrent opinion in virology · 2019Review
- Illuminating the virus life cycle with single-molecule FRET imaging.Advances in virus research · 2019Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Human immunodeficiency virus-1 (HIV-1) envelope protein (Env) and influenza hemagglutinin (HA) are the surface glycoproteins responsible for viral entry into host cells, the first step in the virus life cycle necessary to initiate infection. These glycoproteins exhibit a high degree of sequence variability and glycosylation, which are used as strategies to escape host immune responses. Nonetheless, antibodies with broadly neutralizing activity against these viruses have been isolated that have managed to overcome these barriers. Here, we review recent advances in the structural characterization of these antibodies with their viral antigens that defines a few sites of vulnerability on these viral spikes. These broadly neutralizing antibodies tend to focus their recognition on the sites of similar function between the two viruses: the receptor-binding site and membrane fusion machinery. However, some sites of recognition are unique to the virus neutralized, such as the dense shield of oligomannose carbohydrates on HIV-1 Env. These observations are discussed in the context of structure-based design strategies to aid in vaccine design or development of antivirals.
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What OpenQuestion holds
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.