Abstract
Helicobacter pylori infections cause gastric ulcers and play a major role in the development of gastric cancer. In 2001, the first protein interactome was published for this species, revealing over 1500 binary protein interactions resulting from 261 yeast two-hybrid screens. Here we roughly double the number of previously published interactions using an ORFeome-based, proteome-wide yeast two-hybrid screening strategy. We identified a total of 1515 protein-protein interactions, of which 1461 are new. The integration of all the interactions reported in H. pylori results in 3004 unique interactions that connect about 70% of its proteome. Excluding interactions of promiscuous proteins we derived from our new data a core network consisting of 908 interactions. We compared our data set to several other bacterial interactomes and experimentally benchmarked the conservation of interactions using 365 protein pairs (interologs) of E. coli of which one third turned out to be conserved in both species.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1318-1329 |
| Number of pages | 12 |
| Journal | Molecular and Cellular Proteomics |
| Volume | 13 |
| Issue number | 5 |
| DOIs | |
| State | Published - 2014 |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Analytical Chemistry
- Medicine(all)
Cite this
A second-generation protein-protein interaction network of helicobacter pylori. / Hauser, Roman; Ceol, Arnaud; Rajagopala, Seesandra V.; Mosca, Roberto; Siszler, Gabriella; Wermke, Nadja; Sikorski, Patricia; Schwarz, Frank; Schick, Matthias; Wuchty, Stefan; Aloy, Patrick; Uetz, Peter.
In: Molecular and Cellular Proteomics, Vol. 13, No. 5, 2014, p. 1318-1329.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A second-generation protein-protein interaction network of helicobacter pylori
AU - Hauser, Roman
AU - Ceol, Arnaud
AU - Rajagopala, Seesandra V.
AU - Mosca, Roberto
AU - Siszler, Gabriella
AU - Wermke, Nadja
AU - Sikorski, Patricia
AU - Schwarz, Frank
AU - Schick, Matthias
AU - Wuchty, Stefan
AU - Aloy, Patrick
AU - Uetz, Peter
PY - 2014
Y1 - 2014
N2 - Helicobacter pylori infections cause gastric ulcers and play a major role in the development of gastric cancer. In 2001, the first protein interactome was published for this species, revealing over 1500 binary protein interactions resulting from 261 yeast two-hybrid screens. Here we roughly double the number of previously published interactions using an ORFeome-based, proteome-wide yeast two-hybrid screening strategy. We identified a total of 1515 protein-protein interactions, of which 1461 are new. The integration of all the interactions reported in H. pylori results in 3004 unique interactions that connect about 70% of its proteome. Excluding interactions of promiscuous proteins we derived from our new data a core network consisting of 908 interactions. We compared our data set to several other bacterial interactomes and experimentally benchmarked the conservation of interactions using 365 protein pairs (interologs) of E. coli of which one third turned out to be conserved in both species.
AB - Helicobacter pylori infections cause gastric ulcers and play a major role in the development of gastric cancer. In 2001, the first protein interactome was published for this species, revealing over 1500 binary protein interactions resulting from 261 yeast two-hybrid screens. Here we roughly double the number of previously published interactions using an ORFeome-based, proteome-wide yeast two-hybrid screening strategy. We identified a total of 1515 protein-protein interactions, of which 1461 are new. The integration of all the interactions reported in H. pylori results in 3004 unique interactions that connect about 70% of its proteome. Excluding interactions of promiscuous proteins we derived from our new data a core network consisting of 908 interactions. We compared our data set to several other bacterial interactomes and experimentally benchmarked the conservation of interactions using 365 protein pairs (interologs) of E. coli of which one third turned out to be conserved in both species.
UR - http://www.scopus.com/inward/record.url?scp=84899736443&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84899736443&partnerID=8YFLogxK
U2 - 10.1074/mcp.O113.033571
DO - 10.1074/mcp.O113.033571
M3 - Article
C2 - 24627523
AN - SCOPUS:84899736443
VL - 13
SP - 1318
EP - 1329
JO - Molecular and Cellular Proteomics
JF - Molecular and Cellular Proteomics
SN - 1535-9476
IS - 5
ER -