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Database Profile

DBSecSys 2.0

General information

URL: http://dbsecsys.bhsai.org
Full name:
Description: The Database of Burkholderia Secretion Systems 2.0 (DBSecSys 2.0) contains a curated set of 204 Burkholderia mallei (strain ATCC 23344) and 281 Burkholderia pseudomallei (strain K96243) proteins, which are either associated with 5 secretion systems or are known to be secreted but their secretion system type is undetermined. For these proteins, 170 B. mallei proteins are associated with 12 inferred pathogen mechanisms of action and 179 B. pseudomallei proteins are associated with 13 inferred pathogen mechanisms of action. Additionally, DBSecSys 2.0 contains more than 4,500 host-pathogen interactions between human/murine proteins and bacterial proteins associated with secretion systems.
Year founded: 2014
Last update:
Version: 2.0
Accessibility:
Accessible
Country/Region: United States

Classification & Tag

Data type:
Data object:
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Keywords:

Contact information

University/Institution: Biotechnology High Performance Computing Software Applications Institute
Address: Department of Defense Biotechnology High Performance Computing Software Applications Institute, Telemedicine and Advanced Technology Research Center, U.S. Army Medical Research and Materiel Command, Fort Detrick, MD 21702 USA
City:
Province/State:
Country/Region: United States
Contact name (PI/Team): Jaques Reifman
Contact email (PI/Helpdesk): jaques.reifman.civ@mail.mil

Publications

27650316
DBSecSys 2.0: a database of Burkholderia mallei and Burkholderia pseudomallei secretion systems. [PMID: 27650316]
Memišević V, Kumar K, Zavaljevski N, DeShazer D, Wallqvist A, Reifman J.

BACKGROUND: Burkholderia mallei and B. pseudomallei are the causative agents of glanders and melioidosis, respectively, diseases with high morbidity and mortality rates. B. mallei and B. pseudomallei are closely related genetically; B. mallei evolved from an ancestral strain of B. pseudomallei by genome reduction and adaptation to an obligate intracellular lifestyle. Although these two bacteria cause different diseases, they share multiple virulence factors, including bacterial secretion systems, which represent key components of bacterial pathogenicity. Despite recent progress, the secretion system proteins for B. mallei and B. pseudomallei, their pathogenic mechanisms of action, and host factors are not well characterized.
RESULTS: We previously developed a manually curated database, DBSecSys, of bacterial secretion system proteins for B. mallei. Here, we report an expansion of the database with corresponding information about B. pseudomallei. DBSecSys 2.0 contains comprehensive literature-based and computationally derived information about B. mallei ATCC 23344 and literature-based and computationally derived information about B. pseudomallei K96243. The database contains updated information for 163 B. mallei proteins from the previous database and 61 additional B. mallei proteins, and new information for 281 B. pseudomallei proteins associated with 5 secretion systems, their 1,633 human- and murine-interacting targets, and 2,400 host-B. mallei interactions and 2,286 host-B. pseudomallei interactions. The database also includes information about 13 pathogenic mechanisms of action for B. mallei and B. pseudomallei secretion system proteins inferred from the available literature or computationally. Additionally, DBSecSys 2.0 provides details about 82 virulence attenuation experiments for 52 B. mallei secretion system proteins and 98 virulence attenuation experiments for 61 B. pseudomallei secretion system proteins. We updated the Web interface and data access layer to speed-up users' search of detailed information for orthologous proteins related to secretion systems of the two pathogens.
CONCLUSIONS: The updates of DBSecSys 2.0 provide unique capabilities to access comprehensive information about secretion systems of B. mallei and B. pseudomallei. They enable studies and comparisons of corresponding proteins of these two closely related pathogens and their host-interacting partners. The database is available at http://dbsecsys.bhsai.org .

BMC Bioinformatics. 2016:17() | 4 Citations (from Europe PMC, 2025-03-29)
25030112
DBSecSys: a database of Burkholderia mallei secretion systems. [PMID: 25030112]
Memišević V, Kumar K, Cheng L, Zavaljevski N, DeShazer D, Wallqvist A, Reifman J.

BACKGROUND: Bacterial pathogenicity represents a major public health concern worldwide. Secretion systems are a key component of bacterial pathogenicity, as they provide the means for bacterial proteins to penetrate host-cell membranes and insert themselves directly into the host cells' cytosol. Burkholderia mallei is a Gram-negative bacterium that uses multiple secretion systems during its host infection life cycle. To date, the identities of secretion system proteins for B. mallei are not well known, and their pathogenic mechanisms of action and host factors are largely uncharacterized.
DESCRIPTION: We present the Database of Burkholderia malleiSecretion Systems (DBSecSys), a compilation of manually curated and computationally predicted bacterial secretion system proteins and their host factors. Currently, DBSecSys contains comprehensive experimentally and computationally derived information about B. mallei strain ATCC 23344. The database includes 143 B. mallei proteins associated with five secretion systems, their 1,635 human and murine interacting targets, and the corresponding 2,400 host-B. mallei interactions. The database also includes information about 10 pathogenic mechanisms of action for B. mallei secretion system proteins inferred from the available literature. Additionally, DBSecSys provides details about 42 virulence attenuation experiments for 27 B. mallei secretion system proteins. Users interact with DBSecSys through a Web interface that allows for data browsing, querying, visualizing, and downloading.
CONCLUSIONS: DBSecSys provides a comprehensive, systematically organized resource of experimental and computational data associated with B. mallei secretion systems. It provides the unique ability to study secretion systems not only through characterization of their corresponding pathogen proteins, but also through characterization of their host-interacting partners.The database is available at https://applications.bhsai.org/dbsecsys.

BMC Bioinformatics. 2014:15() | 8 Citations (from Europe PMC, 2025-03-29)

Ranking

All databases:
4240/6278 (32.478%)
Interaction:
749/1052 (28.897%)
4240
Total Rank
12
Citations
1.2
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Record metadata

Created on: 2018-01-27
Curated by:
huma shireen [2018-08-28]
Farah Nazir [2018-04-12]
Farah Nazir [2018-04-07]