ArticleProceedings of the National Academy of Sciences of the United States of America2013
Viral infection modulation and neutralization by camelid nanobodies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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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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.
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Who cites it
28 citing papers in PubMed, 51 citations in OpenAlex.
- Antiviral activity of intracellular nanobodies targeting the influenza virus RNA-polymerase core.PLoS pathogens · 2024Article
- Structural flexibility of Toscana virus nucleoprotein in the presence of a single-chain camelid antibody.Acta crystallographica. Section D, Structural biology · 2024Article
- Is Dog Owner Obesity a Risk Factor for Canine Obesity? A "One-Health" Study on Human-Animal Interaction in a Region with a High Prevalence of Obesity.Veterinary sciences · 2022Article
- Review
- An overview of some potential immunotherapeutic options against COVID-19.International immunopharmacology · 2021Review
- First insights into the structural features of Ebola virus methyltransferase activities.Nucleic acids research · 2021Article
- Supramolecular assembly of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Coronavirus pandemic: treatment and future prevention.Future microbiology · 2020Article
- Article
- Potential therapeutic targets and promising drugs for combating SARS-CoV-2.British journal of pharmacology · 2020Review
- Therapeutic strategies in an outbreak scenario to treat the novel coronavirus originating in Wuhan, China.F1000Research · 2020Review
- Structure and genome ejection mechanism ofScience advances · 2019Article
- From Desert to Medicine: A Review of Camel Genomics and Therapeutic Products.Frontiers in genetics · 2019Review
- Type IX secretion system PorM and gliding machinery GldM form arches spanning the periplasmic space.Nature communications · 2018Article
- Unraveling the Self-Assembly of themBio · 2017Article
- Type VI secretion TssK baseplate protein exhibits structural similarity with phage receptor-binding proteins and evolved to bind the membrane complex.Nature microbiology · 2017Article
- Camelid nanobodies used as crystallization chaperones for different constructs of PorM, a component of the type IX secretion system from Porphyromonas gingivalis.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Distinct antibody species: structural differences creating therapeutic opportunities.Current opinion in immunology · 2016Review
- Article
- Production, crystallization and X-ray diffraction analysis of a complex between a fragment of the TssM T6SS protein and a camelid nanobody.Acta crystallographica. Section F, Structural biology communications · 2015Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Lactococcal phages belong to a large family of Siphoviridae and infect Lactococcus lactis, a gram-positive bacterium used in commercial dairy fermentations. These phages are believed to recognize and bind specifically to pellicle polysaccharides covering the entire bacterium. The phage TP901-1 baseplate, located at the tip of the tail, harbors 18 trimeric receptor binding proteins (RBPs) promoting adhesion to a specific lactococcal strain. Phage TP901-1 adhesion does not require major conformational changes or Ca(2+), which contrasts other lactococcal phages. Here, we produced and characterized llama nanobodies raised against the purified baseplate and the Tal protein of phage TP901-1 as tools to dissect the molecular determinants of phage TP901-1 infection. Using a set of complementary techniques, surface plasmon resonance, EM, and X-ray crystallography in a hybrid approach, we identified binders to the three components of the baseplate, analyzed their affinity for their targets, and determined their epitopes as well as their functional impact on TP901-1 phage infectivity. We determined the X-ray structures of three nanobodies in complex with the RBP. Two of them bind to the saccharide binding site of the RBP and are able to fully neutralize TP901-1 phage infectivity, even after 15 passages. These results provide clear evidence for a practical use of nanobodies in circumventing lactococcal phages viral infection in dairy fermentation.
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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.