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CRP in its structurally altered pentameric conformations also binds to proteins that are denatured and aggregated by immobilization on microtiter plates; however, the identity of the ligand on immobilized proteins remains unknown. We tested the hypotheses that immobilization of proteins generated an amyloid-like structure and that amyloid-like structure was the ligand for structurally altered pentameric CRP. We found that the Abs to amyloid-\u03b2 peptide 1\u201342 (A\u03b2) reacted with immobilized proteins, indicating that some immobilized proteins express an A\u03b2 epitope. Accordingly, four different CRP mutants capable of binding to immobilized proteins were constructed, and their binding to fluid-phase A\u03b2 was determined. All CRP mutants bound to fluid-phase A\u03b2, suggesting that A\u03b2 is a ligand for structurally altered pentameric CRP. In addition, the interaction between CRP mutants and A\u03b2 prevented the formation of A\u03b2 fibrils. The growth of A\u03b2 fibrils was also halted when CRP mutants were added to growing fibrils. Biochemical analyses of CRP mutants revealed altered topology of the Ca2+-binding site, suggesting a role of this region of CRP in binding to A\u03b2. Combined with previous reports that structurally altered pentameric CRP is generated in vivo, we conclude that CRP is a dual pattern recognition molecule and an antiamyloidogenic protein. These findings have implications for Alzheimer\u2019s and other neurodegenerative diseases caused by amyloidosis and for the diseases caused by the deposition of otherwise fluid-phase proteins.<\/jats:p>","DOI":"10.4049\/jimmunol.2200148","type":"journal-article","created":{"date-parts":[[2023,1,3]],"date-time":"2023-01-03T04:12:12Z","timestamp":1672719132000},"page":"1180-1188","source":"Crossref","is-referenced-by-count":12,"title":["Structurally Altered, Not Wild-Type, Pentameric C-Reactive Protein Inhibits Formation of Amyloid-\u03b2 Fibrils"],"prefix":"10.1093","volume":"209","author":[{"given":"Donald N","family":"Ngwa","sequence":"first","affiliation":[{"name":"Department of Biomedical Sciences, Quillen College of Medicine, East Tennessee State University , Johnson City, TN"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alok","family":"Agrawal","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, Quillen College of Medicine, East Tennessee State University , Johnson City, TN"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2022,9,15]]},"reference":[{"key":"2025021008303089500_r1","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1016\/S0969-2126(94)00105-7","article-title":"Comparative analyses of pentraxins: implications for protomer assembly and ligand binding","volume":"2","author":"Srinivasan","year":"1994","journal-title":"Structure"},{"key":"2025021008303089500_r2","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/nsb0496-346","article-title":"Three dimensional structure of human C-reactive protein","volume":"3","author":"Shrive","year":"1996","journal-title":"Nat. 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