Molecular cloning, characterization and expression of the heat shock protein 60 gene from the human pathogenic fungus Paracoccidioides brasiliensis

2001 ◽  
Vol 39 (5) ◽  
pp. 445-455 ◽  
Author(s):  
S. M. S. Izacc ◽  
F. J. Gomez ◽  
R. S. A. Jesuino ◽  
C. A. Fonseca ◽  
M. S. S. Felipe ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Cloning ◽  
Paracoccidioides Brasiliensis ◽  
Pathogenic Fungus ◽  
Heat Shock Protein 60 ◽  
Human Pathogenic Fungus

scholarly journals Vaccination with Heat Shock Protein 60 Induces a Protective Immune Response against Experimental Paracoccidioides brasiliensis Pulmonary Infection

2008 ◽  
Vol 76 (9) ◽  
pp. 4214-4221 ◽  
Author(s):  
Renata de Bastos Ascenço Soares ◽  
Francisco J. Gomez ◽  
Célia Maria de Almeida Soares ◽  
George S. Deepe
Keyword(s):  
Immune Response ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Paracoccidioides Brasiliensis ◽  
Humoral Response ◽  
Interleukin 12 ◽  
Heat Shock Protein 60 ◽  
Lethal Challenge ◽  
Immunodominant Antigen ◽  
Ifn Γ

ABSTRACT Paracoccidioides brasiliensis causes a chronic granulomatous mycosis prevalent in Latin America. The successful resolution of infection with this fungus is dependent on the activation of cellular immunity. We previously identified heat shock protein 60 (HSP60) as a target of the humoral response in paracoccidioidomycosis. Herein we expressed the gene encoding HSP60 in Escherichia coli and analyzed the immunological activity of this recombinant antigen. The immunization of BALB/c mice with recombinant protein emulsified in adjuvant stimulated a cellular immune response. Splenocytes from immunized mice proliferated in response to antigen and released interleukin-12 and gamma interferon (IFN-γ). Vaccination with HSP60 reduced the fungal burden in mice given 106 or 107 yeasts and protected mice from a lethal challenge. The efficacy of the vaccination was blunted by the neutralization of IFN-γ. CD4+ cells were necessary for the efficacy of the vaccination in both the afferent and efferent phases. Thus, we have demonstrated that this immunodominant antigen is a candidate for the development of a vaccine against this fungus.

Molecular cloning, sequence analysis and stress-related changes of the heat shock protein 60 gene in Neobenedenia melleni

2013 ◽  
Vol 33 (6) ◽  
pp. 603-608 ◽  
Author(s):  
Fang WANG ◽  
Jiong CHEN ◽  
Yu-Hong SHI ◽  
Xin-Jiang LU ◽  
Ming-Yun LI
Keyword(s):  
Sequence Analysis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Cloning ◽  
Heat Shock Protein 60

scholarly journals Molecular cloning, characterization and expression of the heat shock protein 60 gene from the human pathogenic fungusParacoccidioides brasiliensis

2001 ◽  
Vol 39 (5) ◽  
pp. 445-455 ◽  
Author(s):  
S. M. S. Izacc ◽  
F. J. Gomez ◽  
R. S. A. Jesuino ◽  
C. A. Fonseca ◽  
M. S. S. Felipe ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Cloning ◽  
Heat Shock Protein 60

Molecular cloning, characterization and expression patterns of heat shock protein 60 (HSP60) in the laying duck (Anas platyrhynchos)

2012 ◽  
Vol 92 (4) ◽  
pp. 425-432 ◽  
Author(s):  
Deqian Wang ◽  
Lizhi Lu ◽  
Yong Tian ◽  
Jinjun Li ◽  
Junda Shen ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Cloning ◽  
Anas Platyrhynchos ◽  
Expression Patterns ◽  
Recovery Period ◽  
Heat Shock Protein 60 ◽  
Post Challenge ◽  
Expression Levels ◽  
Long Term Treatment

Wang, D., Lu, L., Tian, Y., Li, J., Shen, J., Tao, Z., Li, G. and Xu, N. 2012. Molecular cloning, characterization and expression patterns of heat shock protein 60 (HSP60) in the laying duck (Anas platyrhynchos). Can. J. Anim. Sci. 92: 425–432. In the present study, we cloned and characterized the HSP60 cDNA from Anas platyrhyncho (designated as ApHSP60) using a combination of homology and rapid amplification of cDNA ends (RACE). The full-length of ApHSP60 is 2027 bp in length, with an open reading frame of 1707 bp encoding a putative protein of 569 amino acids. Comparison of amino acid sequences of HSP60 revealed ApHSP60 is highly conserved, especially in the domains of classical HSP60 family signatures. ApHSP60 transcripts were at low expression levels throughout embryo development. ApHSP60 transcripts were constitutively expressed in all tested tissues of untreated laying duck, with a maximum level in the liver. Fluorescent real-time quantitative reverse transcription-polymerase chain reaction was applied to determine ApHSP60 expression after exposure to different thermal shocks. Under long term treatment with both 30°C and 35°C, ApHSP60 transcripts in heart and liver were significantly up-regulated. Otherwise, ApHSP60 transcripts were remarkably down-regulated in heart and liver under acute challenge with 40°C (a fatal temperature for laying duck). A time-dependent expression pattern of ApHSP60 was found in the recovery period after heat shock reaction. ApHSP60 expression levels in liver and heart were immediately up-regulated to the maximum at 1 h post-challenge, and then decreased to pre-challenge levels by 2 h and 3 h post-challenge, respectively. These results suggest that mRNA expression of the ApHSP60 gene is constitutive and inducible. Meanwhile, it plays an important role in response to heat stressors.

106 Antibodies against heat-shock protein 60 and 65 in patients with heart failure

2003 ◽  
Vol 2 (1) ◽  
pp. 13
Author(s):  
L JANOSKUTI ◽  
A ZSARY ◽  
Z FORHECZ ◽  
K KELTAI ◽  
T FENYVESI ◽  
...  
Keyword(s):  
Heart Failure ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 60 ◽  
Patients With Heart Failure
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