Heat shock protein 40-Gok1 isolation from Toxoplasma gondii RH strain

Coşkun K. A., Özgür A., Otauǧ B., Mungan M., TUTAR Y.

Protein and Peptide Letters, cilt.20, sa.12, ss.1294-1301, 2013 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 20 Sayı: 12
  • Basım Tarihi: 2013
  • Doi Numarası: 10.2174/092986652012131112113608
  • Dergi Adı: Protein and Peptide Letters
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1294-1301
  • Anahtar Kelimeler: Heat Shock protein 40, Protein aggregation, Protein folding, Toxoplasma gondii
  • Recep Tayyip Erdoğan Üniversitesi Adresli: Hayır

Özet

Toxoplasma gondii is ubiquitous obligate intracellular parasite and is one of the most important pathogen for humans and animals. In humans, T. gondii has two life forms: tachyzoites and bradyzoites. Tachyzoites form of T. gondii can cause acute infection, and it is called toxoplasmosis. The development of latent bradyzoites from rapidly growing tachyzoites has been linked to cellular and environmental stresses which are associated with heat shock proteins (Hsps). Hsps play a protective role against stressors. Hsp40 is an important member of Hsp family and T. gondii has 36 predicted Hsp40 family members. Therefore, we studied the cloning and biochemical characterization of the T. gondii RH strain Hsp40 protein-Gok1. Hsp40 prevents protein aggregation and induce refolding. Consequently, Hsp40s may play essential roles in the mechanisms of bradyzoite development and survival in the host organism. Hsp40-Gok1 functional and structural properties may facilitate drug design and protein targeting against toxoplasmosis. © 2013 Bentham Science Publishers.