Bacteria use structural imperfect mimicry to hijack the host interactome
PLoS Computational Biology, ISSN: 1553-7358, Vol: 16, Issue: 12, Page: e1008395
2020
- 10Citations
- 29Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations10
- Citation Indexes10
- 10
- CrossRef3
- Captures29
- Readers29
- 29
Article Description
Bacteria use protein-protein interactions to infect their hosts and hijack fundamental pathways, which ensures their survival and proliferation. Hence, the infectious capacity of the pathogen is closely related to its ability to interact with host proteins. Here, we show that hubs in the host-pathogen interactome are isolated in the pathogen network by adapting the geometry of the interacting interfaces. An imperfect mimicry of the eukaryotic interfaces allows pathogen proteins to actively bind to the host's target while preventing deleterious effects on the pathogen interactome. Understanding how bacteria recognize eukaryotic proteins may pave the way for the rational design of new antibiotic molecules.
Bibliographic Details
10.1371/journal.pcbi.1008395; 10.1371/journal.pcbi.1008395.g003; 10.1371/journal.pcbi.1008395.g001; 10.1371/journal.pcbi.1008395.g002; 10.1371/journal.pcbi.1008395.g004
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85097678725&origin=inward; http://dx.doi.org/10.1371/journal.pcbi.1008395; http://www.ncbi.nlm.nih.gov/pubmed/33275611; https://dx.plos.org/10.1371/journal.pcbi.1008395.g003; http://dx.doi.org/10.1371/journal.pcbi.1008395.g003; https://dx.plos.org/10.1371/journal.pcbi.1008395.g001; http://dx.doi.org/10.1371/journal.pcbi.1008395.g001; https://dx.plos.org/10.1371/journal.pcbi.1008395; https://dx.plos.org/10.1371/journal.pcbi.1008395.g002; http://dx.doi.org/10.1371/journal.pcbi.1008395.g002; https://dx.plos.org/10.1371/journal.pcbi.1008395.g004; http://dx.doi.org/10.1371/journal.pcbi.1008395.g004; https://dx.doi.org/10.1371/journal.pcbi.1008395.g004; https://journals.plos.org/ploscompbiol/article/figure?id=10.1371/journal.pcbi.1008395.g004; https://dx.doi.org/10.1371/journal.pcbi.1008395.g003; https://journals.plos.org/ploscompbiol/article/figure?id=10.1371/journal.pcbi.1008395.g003; https://dx.doi.org/10.1371/journal.pcbi.1008395.g002; https://journals.plos.org/ploscompbiol/article/figure?id=10.1371/journal.pcbi.1008395.g002; https://dx.doi.org/10.1371/journal.pcbi.1008395; https://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.1008395; https://dx.doi.org/10.1371/journal.pcbi.1008395.g001; https://journals.plos.org/ploscompbiol/article/figure?id=10.1371/journal.pcbi.1008395.g001; https://journals.plos.org/ploscompbiol/article/file?id=10.1371/journal.pcbi.1008395&type=printable
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