ArticleInfection and immunity2010
LT-IIc, a new member of the type II heat-labile enterotoxin family encoded by an Escherichia coli strain obtained from a nonmammalian host.
Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- Protective antibodies against enterotoxigenic Escherichia coli are generated from heat-labile toxoid vaccination and exhibit subject- and vaccine-specific diversity.Medical microbiology and immunology · 2025Trial
- Genomic profiling of enterotoxigenicMicrobial genomics · 2025Article
- Article
- Construction of the ETECFinder database for the characterization of enterotoxigenicJournal of clinical microbiology · 2024Article
- The diverse landscape of AB5-type toxins.Engineering microbiology · 2023Review
- Escherichia coli ST131 Associated with Increased Mortality in Bloodstream Infections from Urinary Tract Source.Journal of clinical microbiology · 2023Article
- Characterization of the ganglioside recognition profile of Escherichia coli heat-labile enterotoxin LT-IIc.Glycobiology · 2022Article
- Design of a multi-epitope vaccine against SARS-CoV-2 using immunoinformatics approach.International journal of biological macromolecules · 2020Article
- Towards the first multi-epitope recombinant vaccine against Crimean-Congo hemorrhagic fever virus: A computer-aided vaccine design approach.Journal of biomedical informatics · 2019Article
- Review of Newly Identified Functions Associated With the Heat-Labile Toxin of EnterotoxigenicFrontiers in cellular and infection microbiology · 2019Review
- LT-IIc, A Bacterial Type II Heat-Labile Enterotoxin, Induces Specific Lethality in Triple Negative Breast Cancer Cells by Modulation of Autophagy and Induction of Apoptosis and Necroptosis.International journal of molecular sciences · 2018Article
- Diarrheagenic Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2016Review
- The chromosomal nature of LT-II enterotoxins solved: a lambdoid prophage encodes both LT-II and one of two novel pertussis-toxin-like toxin family members in type II enterotoxigenic Escherichia coli.Pathogens and disease · 2016Article
- Article
- Article
- Recent advances in understanding enteric pathogenic Escherichia coli.Clinical microbiology reviews · 2013Review
- Type II heat-labile enterotoxins: structure, function, and immunomodulatory properties.Veterinary immunology and immunopathology · 2013Review
- Ganglioside-binding specificities of E. coli enterotoxin LT-IIc: Importance of long-chain fatty acyl ceramide.Glycobiology · 2013Article
- Article
- TLR2-dependent modulation of dendritic cells by LT-IIa-B5, a novel mucosal adjuvant derived from a type II heat-labile enterotoxin.Journal of leukocyte biology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Two families of bacterial heat-labile enterotoxins (HLTs) have been described: the type I HLTs are comprised of cholera toxin (CT) of Vibrio cholerae, LT-I of Escherichia coli, and several related HLTs; the type II HLTs are comprised of LT-IIa and LT-IIb. Herein, we report LT-IIc, a new type II HLT encoded from an enterotoxigenic E. coli (ETEC) strain isolated from an avian host. Using a mouse Y1 adrenal cell bioassay, LT-IIc was shown to be less cytotoxic than CT, LT-IIa, or LT-IIb. Cytotoxicity of LT-IIc was partially neutralized by antisera recognizing LT-IIa or LT-IIb but not by anti-CT antiserum. Genes encoding putative A polypeptide and B polypeptides of LT-IIc were arranged in an operon which was flanked by potential prophage sequences. Analysis of the nucleotide and predicted amino acid sequences demonstrated that the A polypeptide of LT-IIc has moderate homology to the A polypeptides of CT and LT-I and high homology to the A polypeptides of LT-IIa and LT-IIb. The B polypeptide of LT-IIc exhibited no significant homology to the B polypeptides of CT and LT-I and only moderate homology to the B polypeptides of LT-IIa and LT-IIb. The binding pattern of LT-IIc for gangliosides was distinctive from that of either LT-IIa or LT-IIb. The data suggest that other types of the type II HLT subfamily are circulating in the environment and that host specificity of type II HLT is likely governed by changes in the B polypeptide which mediate binding to receptors.
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