CalY is a major virulence factor and a biofilm matrix protein. Issue 6 (15th April 2019)
- Record Type:
- Journal Article
- Title:
- CalY is a major virulence factor and a biofilm matrix protein. Issue 6 (15th April 2019)
- Main Title:
- CalY is a major virulence factor and a biofilm matrix protein
- Authors:
- Candela, Thomas
Fagerlund, Annette
Buisson, Christophe
Gilois, Nathalie
Kolstø, Anne‐Brit
Økstad, Ole Andreas
Aymerich, Stéphane
Nielsen‐Leroux, Christina
Lereclus, Didier
Gohar, Michel - Abstract:
- Summary: The extracellular biofilm matrix often contains a network of amyloid fibers which, in the human opportunistic pathogen Bacillus cereus, includes the two homologous proteins TasA and CalY. We show here, in the closely related entomopathogenic species Bacillus thuringiensis, that CalY also displays a second function. In the early stationary phase of planktonic cultures, CalY was located at the bacterial cell‐surface, as shown by immunodetection. Deletion of calY revealed that this protein plays a major role in adhesion to HeLa epithelial cells, to the insect Galleria mellonella hemocytes and in the bacterial virulence against larvae of this insect, suggesting that CalY is a cell‐surface adhesin. In mid‐stationary phase and in biofilms, the location of CalY shifted from the cell surface to the extracellular medium, where it was found as fibers. The transcription study and the deletion of sipW suggested that CalY change of location is due to a delayed activity of the SipW signal peptidase. Using purified CalY, we found that the protein polymerization occurred only in the presence of cell‐surface components. CalY is, therefore, a bifunctional protein, which switches from a cell‐surface adhesin activity in early stationary phase, to the production of fibers in mid‐stationary phase and in biofilms. Abstract : CalY is a biofilm protein produced in high quantities. We found that in early stationary phase, this protein is located at the cell surface where it promotes theSummary: The extracellular biofilm matrix often contains a network of amyloid fibers which, in the human opportunistic pathogen Bacillus cereus, includes the two homologous proteins TasA and CalY. We show here, in the closely related entomopathogenic species Bacillus thuringiensis, that CalY also displays a second function. In the early stationary phase of planktonic cultures, CalY was located at the bacterial cell‐surface, as shown by immunodetection. Deletion of calY revealed that this protein plays a major role in adhesion to HeLa epithelial cells, to the insect Galleria mellonella hemocytes and in the bacterial virulence against larvae of this insect, suggesting that CalY is a cell‐surface adhesin. In mid‐stationary phase and in biofilms, the location of CalY shifted from the cell surface to the extracellular medium, where it was found as fibers. The transcription study and the deletion of sipW suggested that CalY change of location is due to a delayed activity of the SipW signal peptidase. Using purified CalY, we found that the protein polymerization occurred only in the presence of cell‐surface components. CalY is, therefore, a bifunctional protein, which switches from a cell‐surface adhesin activity in early stationary phase, to the production of fibers in mid‐stationary phase and in biofilms. Abstract : CalY is a biofilm protein produced in high quantities. We found that in early stationary phase, this protein is located at the cell surface where it promotes the bacterium binding to host cells. Later, in mid‐ or late stationary phase, CalY is released in the extracellular medium by the signal peptidase SipW and polymerizes as fibers promoting biofilm formation. … (more)
- Is Part Of:
- Molecular microbiology. Volume 111:Issue 6(2019)
- Journal:
- Molecular microbiology
- Issue:
- Volume 111:Issue 6(2019)
- Issue Display:
- Volume 111, Issue 6 (2019)
- Year:
- 2019
- Volume:
- 111
- Issue:
- 6
- Issue Sort Value:
- 2019-0111-0006-0000
- Page Start:
- 1416
- Page End:
- 1429
- Publication Date:
- 2019-04-15
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.14184 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 14830.xml