ArticleThe Journal of biological chemistry2008
alpha-Macroglobulins are present in some gram-negative bacteria: characterization of the alpha2-macroglobulin from Escherichia coli.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Review
- Naming the alpha-2-macroglobulin gene family across vertebrates.Human genomics · 2026Article
- Isolation and Endopeptidase Inhibition of Human α 2-Macroglobulin.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Experimental evolution ofMicrobiology spectrum · 2025Article
- Frozen fresh blood plasma preserves the functionality of native human αScientific reports · 2023Article
- Evolution of protease activation and specificity via alpha-2-macroglobulin-mediated covalent capture.Nature communications · 2023Article
- Cryo-EM structures show the mechanistic basis of pan-peptidase inhibition by human αProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Review
- Irradiation of pediatric glioblastoma cells promotes radioresistance and enhances glioma malignancyOncotarget · 2018Article
- Assembly of an atypical α-macroglobulin complex from Pseudomonas aeruginosa.Scientific reports · 2018Article
- Structural and functional insights into Escherichia coli α2-macroglobulin endopeptidase snap-trap inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structure of protease-cleaved Escherichia coli α-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Neutrophil serine proteases in antibacterial defense.Current opinion in microbiology · 2015Review
- Article
- Multi-signal sedimentation velocity analysis with mass conservation for determining the stoichiometry of protein complexes.PloS one · 2013Article
- Conformational states of a bacterial α2-macroglobulin resemble those of human complement C3.PloS one · 2012Article
- Prokaryote-derived protein inhibitors of peptidases: A sketchy occurrence and mostly unknown function.Biochimie · 2010Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
alpha-Macroglobulins (alphaMs) are large glycoproteins that have been identified in a wide range of vertebrate and invertebrate species and are mostly thiol ester containing proteinase inhibitors. A recent analysis of bacterial genomes ( Budd, A., Blandin, S., Levashina, E. A., and Gibson, T. J. (2004) Genome Biol. 5, R38 ) identified many alpha-macroglobulin-like sequences that appear to have been acquired by Gram-negative bacteria from their metazoan hosts. We report the first expression and characterization of such a bacterial alpha-macroglobulin, that from Escherichia coli. This is also the first alpha-macroglobulin to be characterized that is predicted to be membrane-anchored. We found that the 183-kDa protein contains an intact thiol ester, is monomeric, and is localized to the periplasmic space. Reaction with proteinase results in limited cleavage within a bait region, rapid activation of the thiol ester, cross-linking to the attacking proteinase or other available nucleophiles, and partial protection of the proteinase against macromolecular substrates. Given these properties and the co-occurrence of the alphaM gene with one for a repair transglycosylase, this suggests a possible role for bacterial alphaMs in cell defense following host attack. Such a role would make bacterial alphaMs appropriate novel targets for antibiotic drugs.
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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.