Recombinant Brucella abortus Protease HtpX homolog (htpX)
Description
Introduction to Recombinant Brucella abortus Protease HtpX Homolog (HtpX)
Brucella abortus is the causative agent of brucellosis, a widespread zoonotic disease . The bacterium encodes a variety of proteins that contribute to its survival and virulence within the host. Among these proteins is the HtpX homolog, a protease that belongs to the rhomboid family of intramembrane serine proteases .
Characteristics of HtpX
Rhomboid proteases are highly conserved across various life domains. In eukaryotes, their roles are well-defined, but their functions in bacterial physiology are still being elucidated . HtpX, found in Brucella abortus, exhibits proteolytic activity and can cleave model heterologous substrates such as Drosophila melanogaster Gurken and Providencia stuartii TatA .
Key characteristics of HtpX:
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Protease Activity HtpX functions as an active protease, capable of cleaving specific substrates both in vitro and in vivo .
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Inhibition The activity of HtpX can be inhibited by serine protease inhibitors like 3,4-dichloroisocoumarin (DCI) .
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Structural Features HtpX contains a six-transmembrane domain core, typical of rhomboid proteases, along with an additional N-terminal transmembrane domain .
3.1. Proteomic Analysis
A study used shotgun proteomics to compare the proteomes of Brucella abortus mutant strains lacking the rhomboid gene with parental strains. Quantitative proteomics identified approximately 50% of the predicted B. abortus proteome under two experimental conditions, detecting 108 differentially represented proteins .
3.2. Role in Stress Response
The Brucella abortus HtrA protease, a homolog of HtpX, functions as a stress response protease in the periplasmic space, degrading damaged proteins resulting from environmental stresses . A B. abortus htrA mutant displayed a stress response-defective phenotype in vitro, showing increased sensitivity to hydrogen peroxide and the antibiotic puromycin .
3.3. Oxygen-Limiting Conditions
Deletion of rhomboid had no significant effect on virulence assays, but overexpression of rhomboid impaired growth under static conditions, which suggests it impacts denitrification enzymes and/or high oxygen affinity cytochrome c oxidase required for growth in low oxygen tension conditions .
3.4. Impact on Virulence
Deletion of rhomboid had no obvious effect on B. abortus virulence .
3.5. Subcellular Localization
Immunofluorescence and subcellular fractionation studies suggest that RhoX is an inner membrane protease .
Data Tables
Table 1: Sensitivity of B. abortus RWP11 to Stress Factors
| Stress Factor | Parental Strain 2308 | Mutant Strain RWP11 |
|---|---|---|
| Hydrogen Peroxide (H2O2) | Resistant | Sensitive |
| Puromycin | Resistant | Sensitive |
| Elevated Temperature (41°C) | Normal Growth | Restricted Growth |
Table 2: Differentially Represented Proteins Related to Denitrification and Oxidative Phosphorylation
| Protein | Accession Number |
|---|---|
| Nitrous-oxide reductase NosZ | Q2YJW2 |
| Copper-containing nitrite reductase | Q2YJU8 |
| Nitric oxide reductase subunit C (NorC) | Q2YJT6 |
| Nitrate reductase subunit beta (NarH) | Q2YJY3 |
| Nitrate reductase subunit alpha (NarG) | Q2YJY4 |
| Cbb3-type cytochrome c oxidase unit (high oxygen affinity) | Q2YM85 |
Product Specs
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Target Background
KEGG: bmc:BAbS19_I17020
STRING: 430066.BAbS19_I17020
