+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Secretory nucleoside diphosphate kinases from both intra- and extracellular pathogenic bacteria are functionally indistinguishable



Secretory nucleoside diphosphate kinases from both intra- and extracellular pathogenic bacteria are functionally indistinguishable



Microbiology 157(Pt 11): 3024-3035



Nucleoside diphosphate kinase (NDK), responsible for the maintenance of NTP pools, is an ATP-utilizing enzyme secreted by different pathogens. We found that NDK from Salmonella enterica serovar Typhimurium (S. Typhimurium) is also secretory in nature. Secretory NDK is known to play a crucial role in the survival of pathogenic microbes within host cells through their interaction with extracellular ATP. To elucidate this aspect, we assessed the contribution of secretory products containing NDK from intracellular (Mycobacterium tuberculosis and S. Typhimurium) and extracellular (Vibrio cholerae) pathogens to the process of ATP-induced J774 mouse macrophage cell lysis by monitoring lactate dehydrogenase (LDH) release in the culture medium. Compared with an untreated control, our results demonstrate that S. Typhimurium secretory products caused a greater than twofold decrease in LDH release from J774 macrophage cells treated with ATP. Furthermore, the secretory products from an ndk-deleted strain of S. Typhimurium did not display such behaviour. Contrary to this observation, the secretory products containing NDK of V. cholerae were found to be cytotoxic to J774 cells. At the amino acid level, the sequences of both the NDKs (S. Typhimurium and V. cholerae) exhibited 65 % identity, and their biochemical characteristics (autophosphorylation and phosphotransfer activities) were indistinguishable. However, to our surprise, the secretory product of an ndk-deleted strain of S. Typhimurium, when complemented with V. cholerae ndk, was able to prevent ATP-induced cytolysis. Taken together, our results unambiguously imply that the intrinsic properties of secretory NDKs are identical in intra- and extracellular pathogens, irrespective of their mode of manifestation.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 036247121

Download citation: RISBibTeXText

PMID: 21816881

DOI: 10.1099/mic.0.049221-0


Related references

Deoxyribonucleoside kinases activate nucleoside antibiotics in severely pathogenic bacteria. Antimicrobial Agents and ChemoTherapy 51(8): 2726-2732, 2007

Nucleotide Binding to Nucleoside Diphosphate Kinases: X-ray Structure of Human NDPK-A in Complex with ADP and Comparison to Protein Kinases. Journal of Molecular Biology 332(4): 5-26, 2003

X-ray structure of nucleoside diphosphate kinases. Acta Crystallographica Section A Foundations of Crystallography 49(S1): C82-C82, 1993

The human Nm23/nucleoside diphosphate kinases. Journal of Bioenergetics and Biomembranes 32(3): 247-258, 2000

The nucleoside diphosphate kinases 1973-2000. Journal of Bioenergetics and Biomembranes 32(3): 213-214, 2000

The catalytic mechanism of nucleoside diphosphate kinases. Journal of Bioenergetics and Biomembranes 32(3): 237-246, 2000

Quaternary structure of nucleoside diphosphate kinases. Journal of Bioenergetics and Biomembranes 32(3): 227-236, 2000

The catalytic mechanism of nucleoside diphosphate kinases. Journal of Bioenergetics & Biomembranes 32(3): 237-246, 2000

Quaternary structure of nucleoside diphosphate kinases. Journal of Bioenergetics & Biomembranes 32(3): 227-236, 2000

The human Nm23/nucleoside diphosphate kinases. Journal of Bioenergetics & Biomembranes 32(3): 247-258, 2000

Metabolic functions of microbial nucleoside diphosphate kinases. Journal of Bioenergetics & Biomembranes 32(3): 259-267, 2000

Nucleoside diphosphate kinases (NDPKs) in animal development. Cellular and Molecular Life Sciences 72(8): 1447-1462, 2015

Nucleoside mono and diphosphate kinases of Ascaris lumbricoides.. Biochimica et Biophysica Acta. 47: 1, 52-60, 1961

Metabolic functions of microbial nucleoside diphosphate kinases. Journal of Bioenergetics and Biomembranes 32(3): 259-267, 2000

Regulation of cellular functions by nucleoside diphosphate kinases in mammals. Journal of Bioenergetics & Biomembranes 32(3): 309-315, 2000