期刊
SCIENCE ADVANCES
卷 3, 期 8, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.1701440
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资金
- Natural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN 2015-06667, RGPIN 2013-356025, RGPIN 2014-05138, RGPIN 2016-04810]
- Canadian Foundation for Innovation (CFI)
- European Research Council (ERC) [281595, 635928]
- Dutch Science Foundation grant (NWO ECHO) [712.016.002]
- utch Ministry of Education, Culture and Science grant [024.001.035]
- Canadian Institutes of Health Research Foundation operating grant [106612]
- Canadian Institutes of Health Research (CIHR) Fellowship
- PostGraduate Scholarships-Doctoral Program (PGS-D) NSERC Scholarship
- European Research Council (ERC) [281595, 635928] Funding Source: European Research Council (ERC)
Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium Marinomonas primoryensis uses a 1.5-MDa adhesin comprising over 130 domains to position it on ice at the top of the water column for better access to oxygen and nutrients. We have reconstructed this 0.6-mm-long adhesin using a dissect and build structural biology approach and have established complementary roles for its five distinct regions. Domains in region I (RI) tether the adhesin to the type I secretion machinery in the periplasmof the bacteriumand pass it through the outer membrane. RII comprises similar to 120 identical immunoglobulinlike b-sandwich domains that rigidify on binding Ca2+ to project the adhesion regions RIII and RIV into the medium. RIII contains ligand-binding domains that join diatoms and bacteria together in a mixed-species community on the underside of sea ice where incident light is maximal. RIV is the ice-binding domain, and the terminal RV domain contains several repeats-in-toxin motifs and a noncleavable signal sequence that target proteins for export via the type I secretion system. Similar structural architecture is present in the adhesins of many pathogenic bacteria and provides a guide to finding and blocking binding domains to weaken infectivity.
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