Last update 01 Nov 2024

Bacterial DnaK

Last update 01 Nov 2024

Basic Info

Synonyms-

Introduction-

Drugs associated with Bacterial DnaK

SMR peptide

Target

Bacterial DnaK

Mechanism

Bacterial DnaK inhibitors

Active Org.

Morehouse School of Medicine [+1]

Originator Org.-

Active Indication

Staphylococcus Aureus Infections

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

ML076

Target

Bacterial DnaK

Mechanism

Bacterial DnaK inhibitors

Active Org.

Sanford Burnham Prebys Medical Discovery Institute

Originator Org.

Sanford Burnham Prebys Medical Discovery Institute

Active Indication

Bacterial Infections

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with Bacterial DnaK

100 Translational Medicine associated with Bacterial DnaK

0 Patents (Medical) associated with Bacterial DnaK

Literatures (Medical) associated with Bacterial DnaK

28 Mar 2017·Journal of Microbiology and Biotechnology

Interaction of a 22 kDa Peptidyl Prolyl cis/trans Isomerase with the Heat Shock Protein DnaK in Vibrio anguillarum

Article

Author: Kang, Dong Seop ; Kong, In-Soo ; Cho, Hwa Jin ; Lee, Jong Min ; Moon, Soo Young

Peptidyl prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds preceding prolines. We investigated the protein-protein interaction between a 22 kDa PPIase (VaFKBP22, an FK506-binding protein) and the molecular chaperone DnaK derived from Vibrio anguillarum O1 (VaDnaK) using GST pull-down assays and a bacterial two-hybrid system for in vivo and in vitro studies, respectively. Furthermore, we analyzed the three-dimensional structure of the protein-protein interaction. Based on our results, VaFKBP22 appears to act as a cochaperone of VaDnaK, and contributes to protein folding and stabilization via its peptidyl-prolyl cis/trans isomerization activity.

01 Nov 2016·NatureQ1 · CROSS-FIELD

Alternative modes of client binding enable functional plasticity of Hsp70

Q1 · CROSS-FIELD

Article

Author: Bukau, Bernd ; Mashaghi, Alireza ; Kramer, Günter ; Bezrukavnikov, Sergey ; Minde, David P ; Tans, Sander J ; Mayer, Matthias P ; Wentink, Anne S ; Zachmann-Brand, Beate ; Kityk, Roman

The Hsp70 system is a central hub of chaperone activity in all domains of life. Hsp70 performs a plethora of tasks, including folding assistance, protection against aggregation, protein trafficking, and enzyme activity regulation, and interacts with non-folded chains, as well as near-native, misfolded, and aggregated proteins. Hsp70 is thought to achieve its many physiological roles by binding peptide segments that extend from these different protein conformers within a groove that can be covered by an ATP-driven helical lid. However, it has been difficult to test directly how Hsp70 interacts with protein substrates in different stages of folding and how it affects their structure. Moreover, recent indications of diverse lid conformations in Hsp70-substrate complexes raise the possibility of additional interaction mechanisms. Addressing these issues is technically challenging, given the conformational dynamics of both chaperone and client, the transient nature of their interaction, and the involvement of co-chaperones and the ATP hydrolysis cycle. Here, using optical tweezers, we show that the bacterial Hsp70 homologue (DnaK) binds and stabilizes not only extended peptide segments, but also partially folded and near-native protein structures. The Hsp70 lid and groove act synergistically when stabilizing folded structures: stabilization is abolished when the lid is truncated and less efficient when the groove is mutated. The diversity of binding modes has important consequences: Hsp70 can both stabilize and destabilize folded structures, in a nucleotide-regulated manner; like Hsp90 and GroEL, Hsp70 can affect the late stages of protein folding; and Hsp70 can suppress aggregation by protecting partially folded structures as well as unfolded protein chains. Overall, these findings in the DnaK system indicate an extension of the Hsp70 canonical model that potentially affects a wide range of physiological roles of the Hsp70 system.

01 Feb 2014·The Indian journal of medical research

Role of 72 kDa protein of Leptospira interrogans as a diagnostic marker in acute leptospirosis.

Article

Author: Zainul, F Z ; Amran, F ; Riazi, M ; Khalilpour, A ; Bahaman, A R

BACKGROUND & OBJECTIVESLeptospirosis is a widespread zoonotic disease and a public health problem, particularly in tropical and subtropical countries. Varied clinical manifestations of the disease frequently lead to misdiagnosis resulting in life-threatening multi-organ complications. Therefore, early laboratory investigation using an appropriate diagnostic approach is crucial. In the present study, a potential protein marker was identified and evaluated for its usefulness in the serodiagnosis of acute leptospirosis.METHODSLeptospira interrogans serovar Icterohaemorrhagiae (L44), which represents a commonly prevalent serovar in Malaysia, was cultivated for preparation of sequential protein extract (SEQ). SDS-PAGE and immunoblotting were performed with a serum panel comprising confirmed cases of leptospirosis and controls (n=42 each). Identification and characterization of the highest scoring protein from the antigenic band was performed. Subsequently based on the nucleotide coding sequence of the protein, the corresponding recombinant protein was custom-produced. It was then evaluated for sensitivity and specificity by testing against 20 serum samples from leptospirosis patients and 32 from controls.RESULTSAmong the antigenic components, a 72 kDa protein band demonstrated significant sensitivity (83.3%) and specificity (95.2%) for the detection of specific anti-leptospiral IgM antibodies. The protein was identified by mass-spectrometry analysis as heat shock protein DnaK of L. interrogans. Recombinant form of the protein (r72SEQ) showed 85 per cent sensitivity and 81 per cent specificity for the detection of specific anti-leptospiral IgM antibodies.INTERPRETATION & CONCLUSIONSThe findings of our study indicate that a protein (72 kDa) of L. interrogans has the potential utility of being used for the diagnosis of acute leptospirosis. Further studies need to be done to confirm these findings.

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Bacterial DnaK

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