[Improved efficacy of P277 fused to heat shock protein 65 of Mycobacterium tuberculosis against diabetes in nonobese diabetic mice].

Abstract

To improve the efficacy of peptide P277 in preventing autoimmune diabetes, heat shock protein 65 kD (HSP65) of Mycobacterium tuberculosis var. bovis was fused with linear polypeptide epitope of P277 and expressed as soluble protein in Escherichia coli. The fusion protein HSP65-P277 was purified by anion exchange column chromatography and then used to immunize prediabetic NOD mice with three ip inoculations in absence of adjuvants. Serum samples from the immunized mice were collected monthly and the concentration of blood glucose was measured. The study showed that administration of HSP65-P277 to NOD mice could prevent the development of diabetes more efficiently than the peptide P277 itself or HSP65. Fused to heat shock protein 65 of Mycobacterium tuberculosis could improve the efficacy of diabetes prevention of P277 in nonobese diabetic mice. The results suggest the fusion protein of HSP65-P277 would be useful for treating insulin-dependent diabetes mellitus.

• Authors: Aihua Zhu, Yong Lu, Liang Jin, Jie Wu, Taiming Li, Jingjing Liu
• Journal: Sheng wu gong cheng xue bao = Chinese journal of biotechnology (Sheng Wu Gong Cheng Xue Bao) Vol. 24 Issue 4 Pg. 640-5 (Apr 2008) ISSN: 1000-3061 [Print] China
• PMID: 18616176 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Bacterial Proteins
• Chaperonin 60
• Heat-Shock Proteins
• Peptide Fragments
• Recombinant Fusion Proteins
• Vaccines, Synthetic
• heat-shock protein 65, Mycobacterium
• peptide 277, heat shock protein 60
• Chaperonins

Topics

• Animals
• Bacterial Proteins (biosynthesis, genetics, immunology)
• Chaperonin 60
• Chaperonins (biosynthesis, genetics, immunology)
• Diabetes Mellitus, Type 1 (prevention & control)
• Escherichia coli (genetics, metabolism)
• Female
• Heat-Shock Proteins (genetics, immunology)
• Immunization
• Mice
• Mice, Inbred NOD
• Mycobacterium bovis
• Peptide Fragments (biosynthesis, genetics, immunology)
• Random Allocation
• Recombinant Fusion Proteins (biosynthesis, genetics, immunology)
• Vaccines, Synthetic (genetics, immunology)