Stability improvement of the fatty acid binding protein Sm14 from S. mansoni by Cys replacement: Structural and functional characterization of a vaccine candidate

Ramos, Celso Raul Romero; Spisni, Alberto; Oyama, Sílvia Maria Ribeiro; Sforça, Maurício L.; Ramos, Henrique Roman; Vilar, Mônica Magno; Alves, Adriana; Figueredo, R. C. R.; Tendler, Míriam; Zanchin, Nilson Ivo Tonin; Pertinhez, Thelma A.; Ho, Paulo Lee

doi:10.1016/j.bbapap.2008.12.010

Cited by 30 publications

(24 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Intrinsic tryptophan fluorescence was measured with an excitation wavelength set at 285 nm and emission spectra were recorded in the spectral range 310-400 nm. 68 Alternatively, thermal unfolding studies were carried out in the presence of 8 μM ANS. The temperature range tested was between 20 and 70°C.…”

Section: Spectroscopic and Protein Stability Studiesmentioning

confidence: 99%

Structure and Calcium-Binding Activity of LipL32, the Major Surface Antigen of Pathogenic Leptospira sp.

Hauk

Guzzo

Ramos

et al. 2009

Journal of Molecular Biology

Self Cite

View full text Add to dashboard Cite

Section: Spectroscopic and Protein Stability Studiesmentioning

confidence: 99%

Structure and Calcium-Binding Activity of LipL32, the Major Surface Antigen of Pathogenic Leptospira sp.

Hauk

Guzzo

Ramos

et al. 2009

Journal of Molecular Biology

Self Cite

View full text Add to dashboard Cite

“…To date, the fatty acid–binding proteins (FABP-Fh15 and Sm14) have been the only F. hepatica/S. mansoni –common proteins characterized and exploited as a potential dual-vaccine (Ramajo et al, 2001; Vilar et al, 2003; Ramos et al, 2009). However, because F. hepatica and S. mansoni are parasites with great antigenic complexity, it is expected that they possess common proteins other than FABPs that might contribute to serological cross-reactivity.…”

mentioning

confidence: 99%

Fasciola hepatica and Schistosoma mansoni: Identification of Common Proteins by Comparative Proteomic Analysis

Boukli¹,

Delgado²,

Espino³

2011

Journal of Parasitology

View full text Add to dashboard Cite

It is not unusual to find common molecules among parasites of different species, genera, or phyla. When those molecules are antigenic, they may be used for developing drugs or vaccines that simultaneously target different species or genera of parasite. In the present study, we used a proteomic-based approach to identify proteins that are common to adult Fasciola hepatica and Schistosoma mansoni. Whole-worm extracts from each parasite were separated by 2-dimensional electrophoresis (2-DE), and digital images of both proteomes were superimposed using imaging software to identify proteins with identical isoelectric points and molecular weights. Protein identities were determined by mass spectrometry. Imaging and immunoblot analyses identified 28 immunoreactive proteins that are common to both parasites. Among these molecules are antioxidant proteins (thioredoxin and glutathione-S-transferase), glycolytic enzymes (glyceraldehyde 6-phosphate dehydrogenase and enolase), proteolytic enzymes (cathepsin-L and -D), inhibitors (Kunitz-type, Stefin-1), proteins with chaperone activity (heat shock protein 70 and fatty acid–binding protein), and structural proteins (calcium-binding protein, actin, and myosin). Some of the identified proteins could be used to develop drugs and vaccines against fascioliasis and schistosomiasis.

show abstract

“…To date, two candidate vaccines are in clinical trials, including Sh28GT targeting S. hematobium and Sm14 targeting S. mansoni. 5,6 The Sabin Vaccine Institute Product Development Partnership (PDP) is developing a recombinant vaccine comprised of the extracellular domain of the S. mansoni tetraspanin surface antigen known as Sm-TSP-2 ( Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

Biophysical and formulation studies of theSchistosoma mansoniTSP-2 extracellular domain recombinant protein, a lead vaccine candidate antigen for intestinal schistosomiasis

Cheng¹,

Curti²,

Rezende³

et al. 2013

Human Vaccines & Immunotherapeutics

View full text Add to dashboard Cite

Stability improvement of the fatty acid binding protein Sm14 from S. mansoni by Cys replacement: Structural and functional characterization of a vaccine candidate

Cited by 30 publications

References 37 publications

Structure and Calcium-Binding Activity of LipL32, the Major Surface Antigen of Pathogenic Leptospira sp.

Structure and Calcium-Binding Activity of LipL32, the Major Surface Antigen of Pathogenic Leptospira sp.

Fasciola hepatica and Schistosoma mansoni: Identification of Common Proteins by Comparative Proteomic Analysis

Biophysical and formulation studies of theSchistosoma mansoniTSP-2 extracellular domain recombinant protein, a lead vaccine candidate antigen for intestinal schistosomiasis

Contact Info

Product

Resources

About