Faculty Opinions recommendation of Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug.

2010 ◽  
Author(s):  
Leonard Neckers
Keyword(s):  
Plasmodium Falciparum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Drug Target ◽  
Biochemical Characterization ◽  
Heat Shock Protein 90 ◽  
Trypanosoma Evansi ◽  
Candidate Drug ◽  
Protozoan Infections

scholarly journals Heat Shock Protein 90 as a Drug Target against Protozoan Infections

2010 ◽  
Vol 285 (49) ◽  
pp. 37964-37975 ◽  
Author(s):  
Rani Pallavi ◽  
Nainita Roy ◽  
Rishi Kumar Nageshan ◽  
Pinaki Talukdar ◽  
Soundara Raghavan Pavithra ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Drug Target ◽  
Heat Shock Protein 90 ◽  
Protozoan Infections

scholarly journals Functional characterization of heat-shock protein 90 fromOryza sativaand crystal structure of its N-terminal domain

2015 ◽  
Vol 71 (6) ◽  
pp. 688-696 ◽  
Author(s):  
Swetha Raman ◽  
Kaza Suguna
Keyword(s):  
Crystal Structure ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Biochemical Characterization ◽  
Functional Characterization ◽  
Cell Signalling ◽  
Physiological Role ◽  
Heat Shock Protein 90 ◽  
Terminal Domain

Heat-shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that is essential for the normal functioning of eukaryotic cells. It plays crucial roles in cell signalling, cell-cycle control and in maintaining proteome integrity and protein homeostasis. In plants, Hsp90s are required for normal plant growth and development. Hsp90s are observed to be upregulated in response to various abiotic and biotic stresses and are also involved in immune responses in plants. Although there are several studies elucidating the physiological role of Hsp90s in plants, their molecular mechanism of action is still unclear. In this study, biochemical characterization of an Hsp90 protein from rice (Oryza sativa; OsHsp90) has been performed and the crystal structure of its N-terminal domain (OsHsp90-NTD) was determined. The binding of OsHsp90 to its substrate ATP and the inhibitor 17-AAG was studied by fluorescence spectroscopy. The protein also exhibited a weak ATPase activity. The crystal structure of OsHsp90-NTD was solved in complex with the nonhydrolyzable ATP analogue AMPPCP at 3.1 Å resolution. The domain was crystallized by cross-seeding with crystals of the N-terminal domain of Hsp90 fromDictyostelium discoideum, which shares 70% sequence identity with OsHsp90-NTD. This is the second reported structure of a domain of Hsp90 from a plant source.

Purification of heat shock protein 90 from calf uterus and rat liver and characterization of the highly hydrophobic region

1989 ◽  
Vol 992 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Masaomi Iwasaki ◽  
Hiroyuki Saito ◽  
Masahide Yamamoto ◽  
Kenneth S. Korach ◽  
Tsuneyoshi Hirogome ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Rat Liver ◽  
Heat Shock Protein 90 ◽  
Hydrophobic Region ◽  
Highly Hydrophobic

Heat shock protein 90 as a potential drug target against surra

Parasitology ◽  
2014 ◽  
Vol 141 (9) ◽  
pp. 1148-1155 ◽  
Author(s):  
ANKIT K. ROCHANI ◽  
CHANDAN MITHRA ◽  
MEETALI SINGH ◽  
UTPAL TATU
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Drug Target ◽  
Animal Health ◽  
Heat Shock Protein 90 ◽  
Potential Drug Target ◽  
Potential Drug ◽  
Priority List ◽  
Animal Populations ◽  
Animal Trypanosomiasis

SUMMARYTrypanosomiasis is caused by Trypanosoma species which affect both human and animal populations and pose a major threat to developing countries. The incidence of animal trypanosomiasis is on the rise. Surra is a type of animal trypanosomiasis, caused by Trypanosoma evansi, and has been included in priority list B of significant diseases by the World Organization of Animal Health (OIE). Control of surra has been a challenge due to the lack of effective drugs and vaccines and emergence of resistance towards existing drugs. Our laboratory has previously implicated Heat shock protein 90 (Hsp90) from protozoan parasites as a potential drug target and successfully demonstrated efficacy of an Hsp90 inhibitor in cell culture as well as a pre-clinical mouse model of trypanosomiasis. This article explores the role of Hsp90 in the Trypanosoma life cycle and its potential as a drug target. It appears plausible that the repertoire of Hsp90 inhibitors available in academia and industry may have value for treatment of surra and other animal trypanosomiasis.

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