ArticleJournal of bacteriology2005
Llama antibodies against a lactococcal protein located at the tip of the phage tail prevent phage infection.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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
34 citing papers in PubMed, 75 citations in OpenAlex.
- Article
- Nanobody-Based Probes for Subcellular Protein Identification and Visualization.Frontiers in cellular neuroscience · 2020Review
- A bispecific antibody strategy to target multiple type 2 cytokines in asthma.The Journal of allergy and clinical immunology · 2018Article
- Bivalent Llama Single-Domain Antibody Fragments against Tumor Necrosis Factor Have Picomolar Potencies due to Intramolecular Interactions.Frontiers in immunology · 2017Article
- The Presence of Two Receptor-Binding Proteins Contributes to the Wide Host Range of Staphylococcal Twort-Like Phages.Applied and environmental microbiology · 2016Article
- Article
- Dual anti-idiotypic purification of a novel, native-format biparatopic anti-MET antibody with improved in vitro and in vivo efficacy.Scientific reports · 2016Article
- Nanobody-derived nanobiotechnology tool kits for diverse biomedical and biotechnology applications.International journal of nanomedicine · 2016Review
- Neutralisation of HIV-1 cell-cell spread by human and llama antibodies.Retrovirology · 2014Article
- Four individually druggable MET hotspots mediate HGF-driven tumor progression.The Journal of clinical investigation · 2014Article
- Molecular insights on the recognition of a Lactococcus lactis cell wall pellicle by the phage 1358 receptor binding protein.Journal of virology · 2014Article
- Structures and host-adhesion mechanisms of lactococcal siphophages.Frontiers in microbiology · 2014Review
- Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2.Journal of virology · 2013Article
- Viral infection modulation and neutralization by camelid nanobodies.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Review
- Potent and broad neutralization of HIV-1 by a llama antibody elicited by immunization.The Journal of experimental medicine · 2012Article
- Llama antibody fragments recognizing various epitopes of the CD4bs neutralize a broad range of HIV-1 subtypes A, B and C.PloS one · 2012Article
- Population genomics and phylogeography of an Australian dairy factory derived lytic bacteriophage.Genome biology and evolution · 2012Article
- A biparatopic anti-EGFR nanobody efficiently inhibits solid tumour growth.International journal of cancer · 2011Article
- Unraveling lactococcal phage baseplate assembly by mass spectrometry.Molecular & cellular proteomics : MCP · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophage p2 belongs to the most prevalent lactococcal phage group (936) responsible for considerable losses in industrial production of cheese. Immunization of a llama with bacteriophage p2 led to higher titers of neutralizing heavy-chain antibodies (i.e., devoid of light chains) than of the classical type of immunoglobulins. A panel of p2-specific single-domain antibody fragments was obtained using phage display technology, from which a group of potent neutralizing antibodies were identified. The antigen bound by these antibodies was identified as a protein with a molecular mass of 30 kDa, homologous to open reading frame 18 (ORF18) of phage sk1, another 936-like phage for which the complete genomic sequence is available. By the use of immunoelectron microscopy, the protein is located at the tip of the tail of the phage particle. The addition of purified ORF18 protein to a bacterial culture suppressed phage infection. This result and the inhibition of cell lysis by anti-ORF18 protein antibodies support the conclusion that the ORF18 protein plays a crucial role in the interaction of bacteriophage p2 with the surface receptors of Lactococcus lactis.
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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.