ArticlePloS one2012
Conformational states of a bacterial α2-macroglobulin resemble those of human complement C3.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Molecular characterization of thioester-containing proteins inFrontiers in immunology · 2022Article
- Human pregnancy zone protein stabilizes misfolded proteins including preeclampsia- and Alzheimer's-associated amyloid beta peptide.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Plasma proteome changes in cord blood samples from preterm infants.Journal of perinatology : official journal of the California Perinatal Association · 2018Article
- Assembly of an atypical α-macroglobulin complex from Pseudomonas aeruginosa.Scientific reports · 2018Article
- Sulfmyoglobin Conformational Change: A Role in the Decrease of Oxy-Myoglobin Functionality.Biochemistry and biophysics reports · 2016Article
- Association of salivary alpha 2-macroglobulin levels and clinical characteristics in type 2 diabetes.Journal of diabetes investigation · 2016Article
- 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
- Uniqueness of models from small-angle scattering data: the impact of a hydration shell and complementary NMR restraints.Acta crystallographica. Section D, Biological crystallography · 2015Article
- The structure and function of thioester-containing proteins in arthropods.Biophysical reviews · 2014Article
- Article
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6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α(2) macroglobulins (α(2)Ms) are broad-spectrum protease inhibitors that play essential roles in the innate immune system of eukaryotic species. These large, multi-domain proteins are characterized by a broad-spectrum bait region and an internal thioester, which, upon cleavage, becomes covalently associated to the target protease, allowing its entrapment by a large conformational modification. Notably, α(2)Ms are part of a larger protein superfamily that includes proteins of the complement system, such as C3, a multi-domain macromolecule which is also characterized by an internal thioester-carrying domain and whose activation represents the pivotal step in the complement cascade. Recently, α(2)M/C3-like genes were identified in a large number of bacterial genomes, and the Escherichia coli α(2)M homolog (ECAM) was shown to be activated by proteases. In this work, we have structurally characterized ECAM by electron microscopy and small angle scattering (SAXS) techniques. ECAM is an elongated, flexible molecule with overall similarities to C3 in its inactive form; activation by methylamine, chymotrypsin, or elastase induces a conformational modification reminiscent of the one undergone by the transformation of C3 into its active form, C3b. In addition, the proposed C-terminus of ECAM displays high flexibility and different conformations, and could be the recognition site for partner macromolecules. This work sheds light on a potential bacterial defense mechanism that mimics structural rearrangements essential for activation of the complement cascade in eukaryotes, and represents a possible novel target for the development of antibacterials.
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