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An amyloid-forming segment of β2-microglobulin suggests a molecular model for the fibril
Open accessAbstract
In humans suffering from dialysis-related amyloidosis, the protein β2-microglobulin (β2M) is deposited as an amyloid; however, an amyloid of β2M is unknown in mice. β2M sequences from human and mouse are 70% identical, but there is a seven-residue peptide in which six residues differ. This peptide from human β2M forms amyloid in vitro , whereas the mouse peptide does not. Substitution of the human peptide for its counterpart in the mouse sequence results in the formation of amyloid in vitro . These results show that a seven-residue segment of human β2M is sufficient to convert β2M to the amyloid state, and that specific residue interactions are crucial to the conversion. These observations are consistent with a proposed Zipper-spine model for β2M amyloid, in which the spine of the fibril consists of an anhydrous β-sheet.
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Cited by
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Breydo, L., Wu, J. W., & Uversky, V. N. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.002 · Cited by 657
Protein quality in bacterial inclusion bodies
Ventura, S., & Villaverde, A. (2006) · Trends in Biotechnology · doi:10.1016/j.tibtech.2006.02.007 · Cited by 381
Wang, X., Singh, S. K., & Kumar, S. (2010) · Pharmaceutical Research · doi:10.1007/s11095-010-0143-5 · Cited by 79
AmyloGram reveals amyloidogenic potential in stroke thrombus proteomes
Kell, D. B., Doyle, K. M., Salcedo-Sora, J. E., Sekhar, A., Walker, M., & Pretorius, E. (2025) · Biochemical Journal · doi:10.1042/bcj20253317 · Cited by 4
“Other high-scoring proteins included serum amyloid P [71–73], β2-microglobulin [31,74– 77], protein phosphatase 5, the major prion protein [78–80], and transforming growth factor β1 [81].”
Metadata
- Authors
- Ivanova, M. I., Sawaya, M. R., Gingery, M., Attinger, A., & Eisenberg, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-07-12
- Volume
- 101
- Issue
- 29
- Pages
- 10584-10589
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2166067983
- Cited by
- 219
- References
- 0
- FWCI
- 6.56
- Type
- journal article
- Language
- en
- Open access
- green
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- Ivanova, M. I., Sawaya, M. R., Gingery, M., Attinger, A., & Eisenberg, D. (2004). An amyloid-forming segment of β2-microglobulin suggests a molecular model for the fibril. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0403756101
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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