Immunotation of Rv0016c
From DrugPedia: A Wikipedia for Drug discovery
(→B cell Epitopes) |
|||
| (5 intermediate revisions not shown.) | |||
| Line 17: | Line 17: | ||
[[Category:C2D]] | [[Category:C2D]] | ||
[[Category:Mtb Immunotation]] | [[Category:Mtb Immunotation]] | ||
| - | =General=The bacterial divisome is a multiprotein complex. Specific protein-protein interactions specify whether cell division occurs optimally, or whether division is arrested. Little is known about these protein-protein interactions and their regulation in mycobacteria. We have investigated the interrelationship between the products of the Mycobacterium tuberculosis gene cluster Rv0014c-Rv0019c, namely PknA (encoded by Rv0014c) and FtsZ-interacting protein A, FipA (encoded by Rv0019c) and the products of the division cell wall (dcw) cluster, namely FtsZ and FtsQ. M. smegmatis strains depleted in components of the two gene clusters have been complemented with orthologs of the respective genes of M. tuberculosis. Here we identify FipA as an interacting partner of FtsZ and FtsQ and establish that PknA-dependent phosphorylation of FipA on T77 and FtsZ on T343 is required for cell division under oxidative stress. A fipA knockout strain of M. smegmatis is less capable of withstanding oxidative stress than the wild type and showed elongation of cells due to a defect in septum formation. Localization of FtsQ, FtsZ and FipA at mid-cell was also compromised. Growth and survival defects under oxidative stress could be functionally complemented by fipA of M. tuberculosis but not its T77A mutant. Merodiploid strains of M. smegmatis expressing the FtsZ(T343A) showed inhibition of FtsZ-FipA interaction and Z ring formation under oxidative stress. Knockdown of FipA led to elongation of M. tuberculosis cells grown in macrophages and reduced intramacrophage growth. These data reveal a novel role of phosphorylation-dependent protein-protein interactions involving FipA, in the sustenance of mycobacterial cell division under oxidative stress. | + | =General= |
| + | The bacterial divisome is a multiprotein complex. Specific protein-protein interactions specify whether cell division occurs optimally, or whether division is arrested. Little is known about these protein-protein interactions and their regulation in mycobacteria. We have investigated the interrelationship between the products of the Mycobacterium tuberculosis gene cluster Rv0014c-Rv0019c, namely PknA (encoded by Rv0014c) and FtsZ-interacting protein A, FipA (encoded by Rv0019c) and the products of the division cell wall (dcw) cluster, namely FtsZ and FtsQ. M. smegmatis strains depleted in components of the two gene clusters have been complemented with orthologs of the respective genes of M. tuberculosis. Here we identify FipA as an interacting partner of FtsZ and FtsQ and establish that PknA-dependent phosphorylation of FipA on T77 and FtsZ on T343 is required for cell division under oxidative stress. A fipA knockout strain of M. smegmatis is less capable of withstanding oxidative stress than the wild type and showed elongation of cells due to a defect in septum formation. Localization of FtsQ, FtsZ and FipA at mid-cell was also compromised. Growth and survival defects under oxidative stress could be functionally complemented by fipA of M. tuberculosis but not its T77A mutant. Merodiploid strains of M. smegmatis expressing the FtsZ(T343A) showed inhibition of FtsZ-FipA interaction and Z ring formation under oxidative stress. Knockdown of FipA led to elongation of M. tuberculosis cells grown in macrophages and reduced intramacrophage growth. These data reveal a novel role of phosphorylation-dependent protein-protein interactions involving FipA, in the sustenance of mycobacterial cell division under oxidative stress. | ||
Citation: Sureka K, Hossain T, Mukherjee P, Chatterjee P, Datta P, et al. (2010) Novel Role of | Citation: Sureka K, Hossain T, Mukherjee P, Chatterjee P, Datta P, et al. (2010) Novel Role of | ||
| Line 46: | Line 47: | ||
<tr><td>sp|A5PL33</td><td> 31</td><td> 42</td><td> 61</td><td> 9.7</td></tr></table> | <tr><td>sp|A5PL33</td><td> 31</td><td> 42</td><td> 61</td><td> 9.7</td></tr></table> | ||
| + | =Alergen Protein= | ||
| + | Link to [http://www.imtech.res.in/raghava/algpred/ Algpred]<br> | ||
| + | Non Allergen Predicted by AlgPred Server | ||
| + | =Bacterial Toxin Prediction= | ||
| + | Link to [http://www.imtech.res.in/raghava/btxpred/submission.html btxpred]<br> | ||
| + | No Hit Fountd by btxpred server. | ||
| + | =Subcellular Location= | ||
| + | Link to [http://www.imtech.res.in/raghava/tbpred/ TBpred]<br> | ||
| + | INTEGRAL MEMBRANE PROTEIN | ||
| + | =Antigens= | ||
| + | No Hit Found in [http://www.imtech.res.in/raghava/antigendb/keyquery.html AntigenDB]<br> | ||
| + | No. Hit Found in [http://www.iedb.org/ IEDB] | ||
| + | ==B cell Epitopes== | ||
| + | ====BCEpred Analysis==== | ||
| + | |||
| + | Link to [http://www.imtech.res.in/raghava/bcepred/bcepred_submission.html Bcepred] | ||
| + | <br> | ||
| + | Result Predicited by [http://crdd.osdd.net/drugpedia/images/K1.pdf]<br> | ||
| + | |||
| + | ====ABCpred Analysis==== | ||
| + | Link to [http://www.imtech.res.in/raghava/abcpred/ABC_submission.html ABCpred]<br> | ||
| + | Result Predicited by [http://crdd.osdd.net/drugpedia/images/K2.pdf]<br> | ||
| + | |||
| + | ====IEDB Analysis==== | ||
| + | Link to [http://tools.immuneepitope.org/tools/bcell/iedb_input IEDB]<br> | ||
| + | Result Predicited by []<br> | ||
| + | |||
| + | =MHC Class-I Binder= | ||
| + | ==nHLAPred Analysis== | ||
| + | Link to [http://www.imtech.res.in/raghava/nhlapred/comp.html nHLApred] | ||
| + | <br> | ||
| + | Result Predicited by [http://crdd.osdd.net/drugpedia/index.php/Image:Pp.txt]<br> | ||
| + | ==IEDB Analysis== | ||
| + | Link to [http://tools.immuneepitope.org/analyze/html/mhc_processing.html IEDB] <br> | ||
| + | Result Predicted by [http://crdd.osdd.net/drugpedia/index.php/Image:Pp1.txt] | ||
| + | =MHC Class-II Binder= | ||
| + | ==Propred Analysis== | ||
| + | Link to [http://www.imtech.res.in/raghava/propred/ Propred]<br> | ||
| + | Result Predicted by [http://crdd.osdd.net/drugpedia/index.php/Image:Pp2.txt] | ||
| + | ==NetMHC-II Analysis== | ||
| + | Link to [http://www.cbs.dtu.dk/services/NetMHCII/ NetMHC-II]<br> | ||
| + | Result Predicted by [http://crdd.osdd.net/drugpedia/index.php/Image:Pp4.txt] | ||
Current revision
| Immunotation of Rv0016c
| |
| Name | |
| <Rv0015c>transmembrane serine/threonine-protein kinase A pknA | |
| Identifiers | |
| Swiss Prot | |
| Genbank | |
| PDB | |
| Chemical data | |
| Formula | ? |
| Mol. wt. | 45598 |
| Pharmacokinetic data | |
| Bioavailability | ? |
| Solubility | ? |
| Isoelectric-Point | 11.1868 |
Contents |
[edit] General
The bacterial divisome is a multiprotein complex. Specific protein-protein interactions specify whether cell division occurs optimally, or whether division is arrested. Little is known about these protein-protein interactions and their regulation in mycobacteria. We have investigated the interrelationship between the products of the Mycobacterium tuberculosis gene cluster Rv0014c-Rv0019c, namely PknA (encoded by Rv0014c) and FtsZ-interacting protein A, FipA (encoded by Rv0019c) and the products of the division cell wall (dcw) cluster, namely FtsZ and FtsQ. M. smegmatis strains depleted in components of the two gene clusters have been complemented with orthologs of the respective genes of M. tuberculosis. Here we identify FipA as an interacting partner of FtsZ and FtsQ and establish that PknA-dependent phosphorylation of FipA on T77 and FtsZ on T343 is required for cell division under oxidative stress. A fipA knockout strain of M. smegmatis is less capable of withstanding oxidative stress than the wild type and showed elongation of cells due to a defect in septum formation. Localization of FtsQ, FtsZ and FipA at mid-cell was also compromised. Growth and survival defects under oxidative stress could be functionally complemented by fipA of M. tuberculosis but not its T77A mutant. Merodiploid strains of M. smegmatis expressing the FtsZ(T343A) showed inhibition of FtsZ-FipA interaction and Z ring formation under oxidative stress. Knockdown of FipA led to elongation of M. tuberculosis cells grown in macrophages and reduced intramacrophage growth. These data reveal a novel role of phosphorylation-dependent protein-protein interactions involving FipA, in the sustenance of mycobacterial cell division under oxidative stress.
Citation: Sureka K, Hossain T, Mukherjee P, Chatterjee P, Datta P, et al. (2010) Novel Role of
[edit] Protein Sequence
>Rv0016c, TB.seq 18762:20234 MW:51577 MNASLRRISVTVMALIVLLLLNATMTQVFTADGLRADPRNQRVLLDEYSRQRGQITAGGQLLAYSVATDGRFRFLRVYPN PEVYAPVTGFYSLRYSSTALERAEDPILNGSDRRLFGRRLADFFTGRDPRGGNVDTTINPRIQQAGWDAMQQGCYGPCKG AVVALEPSTGKILALVSSPSYDPNLLASHNPEVQAQAWQRLGDNPASPLTNRAISETYPPGSTFKVITTAAALAAGATET EQLTAAPTIPLPGSTAQLENYGGAPCGDEPTVSLREAFVKSCNTAFVQLGIRTGADALRSMARAFGLDSPPRPTPLQVAE STVGPIPDSAALGMTSIGQKDVALTPLANAEIAATIANGGITMRPYLVGSLKGPDLANISTTVGYQQRRAVSPQVAAKLT ELMVGAEKVAQQKGAIPGVQIASKTGTAEHGTDPRHTPPHAWYIAFAPAQAPKVAVAVLVENGADRLSATGGALAAPIGR AVIEAALQGEP
[edit] Human Homologue Blast Result
| subject ids | % identity | % positives | alignment length | evalue |
| sp|O75533 | 32 | 46 | 96 | 0.013 |
| sp|Q8NBJ5 | 50 | 64 | 28 | 5.5 |
| sp|P56715 | 24 | 42 | 142 | 6.5 |
| sp|P98168 | 55 | 65 | 20 | 7.7 |
| sp|A5PL33 | 31 | 42 | 61 | 9.7 |
[edit] Alergen Protein
Link to Algpred
Non Allergen Predicted by AlgPred Server
[edit] Bacterial Toxin Prediction
Link to btxpred
No Hit Fountd by btxpred server.
[edit] Subcellular Location
Link to TBpred
INTEGRAL MEMBRANE PROTEIN
[edit] Antigens
No Hit Found in AntigenDB
No. Hit Found in IEDB
[edit] B cell Epitopes
[edit] BCEpred Analysis
Link to Bcepred
Result Predicited by [1]
[edit] ABCpred Analysis
Link to ABCpred
Result Predicited by [2]
[edit] IEDB Analysis
Link to IEDB
Result Predicited by []
[edit] MHC Class-I Binder
[edit] nHLAPred Analysis
Link to nHLApred
Result Predicited by [3]
[edit] IEDB Analysis
Link to IEDB
Result Predicted by [4]
[edit] MHC Class-II Binder
[edit] Propred Analysis
Link to Propred
Result Predicted by [5]
