Identification of a Unique Amyloid Sequence in AA Amyloidosis of a Pig Associated With Streptococcus Suis Infection
| Autor: | S Yoshimoto, Takayuki Mineshige, Kinji Shirota, Go Sugahara, Junichi Kamiie, K Uetsuka, Naoyuki Aihara |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Pathology medicine.medical_specialty General Veterinary Amyloid 040301 veterinary sciences Amyloidosis Streptococcus suis Peptide 04 agricultural and veterinary sciences Biology medicine.disease biology.organism_classification Molecular biology 0403 veterinary science 03 medical and health sciences 030104 developmental biology AA amyloidosis chemistry medicine Serum amyloid A Peptide sequence Serum Amyloid A Protein |
| Zdroj: | Veterinary Pathology. 54:111-118 |
| ISSN: | 1544-2217 0300-9858 |
| DOI: | 10.1177/0300985816653792 |
| Popis: | Here we report a pig with amyloid A (AA) amyloidosis associated with Streptococcus suis infection and identification of a unique amyloid sequence in the amyloid deposits in the tissue. Tissues from the 180-day-old underdeveloped pig contained foci of necrosis and suppurative inflammation associated with S. suis infection. Congo red stain, immunohistochemistry, and electron microscopy revealed intense AA deposition in the spleen and renal glomeruli. Mass spectrometric analysis of amyloid material extracted from the spleen showed serum AA 2 (SAA2) peptide as well as a unique peptide sequence previously reported in a pig with AA amyloidosis. The common detection of the unique amyloid sequence in the current and past cases of AA amyloidosis in pigs suggests that this amyloid sequence might play a key role in the development of porcine AA amyloidosis. An in vitro fibrillation assay demonstrated that the unique AA peptide formed typically rigid, long amyloid fibrils (10 nm wide) and the N-terminus peptide of SAA2 formed zigzagged, short fibers (7 nm wide). Moreover, the SAA2 peptide formed long, rigid amyloid fibrils in the presence of sonicated amyloid fibrils formed by the unique AA peptide. These findings indicate that the N-terminus of SAA2 as well as the AA peptide mediate the development of AA amyloidosis in pigs via cross-seeding polymerization. |
| Databáze: | OpenAIRE |
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