ArticlePloS one2010
The structure of tumor endothelial marker 8 (TEM8) extracellular domain and implications for its receptor function for recognizing anthrax toxin.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 40 citations in OpenAlex.
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- Waging war against cardiac fibrosis by targeting the anthrax toxin receptor.Nature cardiovascular research · 2025Article
- ANTXR1 blockade enhances cardiac function in preclinical models of heart failure.Nature cardiovascular research · 2025Article
- Elevated expression ofFrontiers in molecular biosciences · 2024Article
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- AB Toxins as High-Affinity Ligands for Cell Targeting in Cancer Therapy.International journal of molecular sciences · 2023Review
- CAR-T cell therapy in triple-negative breast cancer: Hunting the invisible devil.Frontiers in immunology · 2022Review
- N-Linked Glycosylation on Anthrax Toxin Receptor 1 Is Essential for Seneca Valley Virus Infection.Viruses · 2021Article
- Inter-α-inhibitor heavy chain-1 has an integrin-like 3D structure mediating immune regulatory activities and matrix stabilization during ovulation.The Journal of biological chemistry · 2020Article
- Structural and Biophysical Analysis of the CLCA1 VWA Domain Suggests Mode of TMEM16A Engagement.Cell reports · 2020Article
- PASTMUS: mapping functional elements at single amino acid resolution in human cells.Genome biology · 2019Article
- The ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase.The Biochemical journal · 2019Article
- Converging physiological roles of the anthrax toxin receptors.F1000Research · 2019Review
- Seneca Valley virus attachment and uncoating mediated by its receptor anthrax toxin receptor 1.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural basis for anthrax toxin receptor 1 recognition by Seneca Valley Virus.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- TEM8/ANTXR1-Specific CAR T Cells as a Targeted Therapy for Triple-Negative Breast Cancer.Cancer research · 2018Article
- Seneca Valley Virus Exploits TEM8, a Collagen Receptor Implicated in Tumor Growth.Frontiers in oncology · 2018Review
- Article
- Indirubin inhibits cell proliferation, migration, invasion and angiogenesis in tumor-derived endothelial cells.OncoTargets and therapy · 2018Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Anthrax toxin, which is released from the gram-positive bacterium Bacillus anthracis, is composed of three proteins: protective antigen (PA), lethal factor (LF), and edema factor (EF). PA binds a receptor on the surface of the target cell and further assembles into a homo-heptameric pore through which EF and LF translocate into the cytosol. Two distinct cellular receptors for anthrax toxin, TEM8/ANTXR1 and CMG2/ANTXR2, have been identified, and it is known that their extracellular domains bind PA with low and high affinities, respectively. Here, we report the crystal structure of the TEM8 extracellular vWA domain at 1.7 A resolution. The overall structure has a typical integrin fold and is similar to that of the previously published CMG2 structure. In addition, using structure-based mutagenesis, we demonstrate that the putative interface region of TEM8 with PA (consisting of residues 56, 57, and 154-160) is responsible for the PA-binding affinity differences between the two receptors. In particular, Leu56 was shown to be a key factor for the lower affinity of TEM8 towards PA compared with CMG2. Because of its high affinity for PA and low expression in normal tissues, an isolated extracellular vWA domain of the L56A TEM8 variant may serve as a potent antitoxin and a potential therapeutic treatment for anthrax infection. Moreover, as TEM8 is often over-expressed in tumor cells, our TEM8 crystal structure may provide new insights into how to design PA mutants that preferentially target tumor cells.
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