ReviewMicrobiology and molecular biology reviews : MMBR2016
Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria.
Review in Microbiology and molecular biology reviews : MMBR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 138 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
138 citing papers in PubMed, 302 citations in OpenAlex.
- Step-by-step maturation mechanism of the binary toxin pore revealed by cryo-EM analysis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Amino Acid Substitutions in the C-Terminal Domains of Vip3Aa Enhance Insecticidal Toxicity.Biology · 2026Article
- Article
- Structural basis for the assembly and translocation of the Vip1-Vip2 insecticidal toxin from Bacillus thuringiensis.Nature communications · 2026Article
- Multi-trait improvement of sorghum: co-expression ofaBIOTECH · 2026Article
- Article
- Transgenic sugarcane harboringFrontiers in plant science · 2026Article
- Assessment of genetically modified cotton T304-40 × GHB119 × COT102 (application EFSA-GMO-BE-2018-155).EFSA journal. European Food Safety Authority · 2025Article
- Assessment of genetically modified cotton GHB614 × T304-40 × GHB119 × COT102 (application EFSA-GMO-ES-2017-147).EFSA journal. European Food Safety Authority · 2025Article
- Characterization of the spectrum of insecticidal activity of Cry1B.3, Cry1Da_7, and Vip3Cb1 proteins produced by lepidopteran-protected MON 89151 cotton.Scientific reports · 2025Article
- Ecological risk assessment for Cry1Da_7, Cry1B.3 and Vip3Cb1 proteins expressed in MON 89151 cotton: an insect-protected cotton with targeted activity against Lepidoptera.Transgenic research · 2025Article
- Vip3C proteins fromApplied and environmental microbiology · 2025Article
- Integrated genomic and proteomic analysis of local Bacillus thuringiensis isolates for targeted insect pest control and functional insight.Archives of microbiology · 2025Article
- Screening signal peptides from Bacillus thuringiensis secretome for heterologous protein secretion.Applied microbiology and biotechnology · 2025Article
- Disruption of HaVipR1 confers Vip3Aa resistance in the moth crop pest Helicoverpa armigera.PLoS biology · 2025Article
- Impact of codon optimization onFrontiers in plant science · 2025Article
- Bioactive Potential of SomeInsects · 2024Article
- Insights into the structural changes that trigger receptor binding upon proteolytic activation of Bacillus thuringiensis Vip3Aa insecticidal protein.PLoS pathogens · 2024Article
- Mismatch between lab-generated and field-evolved resistance to transgenic Bt crops inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Retrotransposon-mediated disruption of a chitin synthase gene confers insect resistance to Bacillus thuringiensis Vip3Aa toxin.PLoS biology · 2024Article
78 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Entomopathogenic bacteria produce insecticidal proteins that accumulate in inclusion bodies or parasporal crystals (such as the Cry and Cyt proteins) as well as insecticidal proteins that are secreted into the culture medium. Among the latter are the Vip proteins, which are divided into four families according to their amino acid identity. The Vip1 and Vip2 proteins act as binary toxins and are toxic to some members of the Coleoptera and Hemiptera. The Vip1 component is thought to bind to receptors in the membrane of the insect midgut, and the Vip2 component enters the cell, where it displays its ADP-ribosyltransferase activity against actin, preventing microfilament formation. Vip3 has no sequence similarity to Vip1 or Vip2 and is toxic to a wide variety of members of the Lepidoptera. Its mode of action has been shown to resemble that of the Cry proteins in terms of proteolytic activation, binding to the midgut epithelial membrane, and pore formation, although Vip3A proteins do not share binding sites with Cry proteins. The latter property makes them good candidates to be combined with Cry proteins in transgenic plants (Bacillus thuringiensis-treated crops [Bt crops]) to prevent or delay insect resistance and to broaden the insecticidal spectrum. There are commercially grown varieties of Bt cotton and Bt maize that express the Vip3Aa protein in combination with Cry proteins. For the most recently reported Vip4 family, no target insects have been found yet.
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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.