Characterisation of pellicles formed by Acinetobacter baumannii at the air-liquid interface.
The clinical importance of Acinetobacter baumannii is partly due to its natural ability to survive in the hospital environment. This persistence may be explained by its capacity to form biofilms and, interestingly, A. baumannii can form pellicles at the air-liquid interface more readily than other l...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4216135?pdf=render |
| _version_ | 1818362840718770176 |
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| author | Yassine Nait Chabane Sara Marti Christophe Rihouey Stéphane Alexandre Julie Hardouin Olivier Lesouhaitier Jordi Vila Jeffrey B Kaplan Thierry Jouenne Emmanuelle Dé |
| author_facet | Yassine Nait Chabane Sara Marti Christophe Rihouey Stéphane Alexandre Julie Hardouin Olivier Lesouhaitier Jordi Vila Jeffrey B Kaplan Thierry Jouenne Emmanuelle Dé |
| author_sort | Yassine Nait Chabane |
| collection | DOAJ |
| description | The clinical importance of Acinetobacter baumannii is partly due to its natural ability to survive in the hospital environment. This persistence may be explained by its capacity to form biofilms and, interestingly, A. baumannii can form pellicles at the air-liquid interface more readily than other less pathogenic Acinetobacter species. Pellicles from twenty-six strains were morphologically classified into three groups: I) egg-shaped (27%); II) ball-shaped (50%); and III) irregular pellicles (23%). One strain representative of each group was further analysed by Brewster's Angle Microscopy to follow pellicle development, demonstrating that their formation did not require anchoring to a solid surface. Total carbohydrate analysis of the matrix showed three main components: Glucose, GlcNAc and Kdo. Dispersin B, an enzyme that hydrolyzes poly-N-acetylglucosamine (PNAG) polysaccharide, inhibited A. baumannii pellicle formation, suggesting that this exopolysaccharide contributes to pellicle formation. Also associated with the pellicle matrix were three subunits of pili assembled by chaperon-usher systems: the major CsuA/B, A1S_1510 (presented 45% of identity with the main pilin F17-A from enterotoxigenic Escherichia coli pili) and A1S_2091. The presence of both PNAG polysaccharide and pili systems in matrix of pellicles might contribute to the virulence of this emerging pathogen. |
| first_indexed | 2024-12-13T21:38:59Z |
| format | Article |
| id | doaj.art-bad1b2464e0c4dad91e0e33c0fa552d8 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-13T21:38:59Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-bad1b2464e0c4dad91e0e33c0fa552d82022-12-21T23:30:37ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-01910e11166010.1371/journal.pone.0111660Characterisation of pellicles formed by Acinetobacter baumannii at the air-liquid interface.Yassine Nait ChabaneSara MartiChristophe RihoueyStéphane AlexandreJulie HardouinOlivier LesouhaitierJordi VilaJeffrey B KaplanThierry JouenneEmmanuelle DéThe clinical importance of Acinetobacter baumannii is partly due to its natural ability to survive in the hospital environment. This persistence may be explained by its capacity to form biofilms and, interestingly, A. baumannii can form pellicles at the air-liquid interface more readily than other less pathogenic Acinetobacter species. Pellicles from twenty-six strains were morphologically classified into three groups: I) egg-shaped (27%); II) ball-shaped (50%); and III) irregular pellicles (23%). One strain representative of each group was further analysed by Brewster's Angle Microscopy to follow pellicle development, demonstrating that their formation did not require anchoring to a solid surface. Total carbohydrate analysis of the matrix showed three main components: Glucose, GlcNAc and Kdo. Dispersin B, an enzyme that hydrolyzes poly-N-acetylglucosamine (PNAG) polysaccharide, inhibited A. baumannii pellicle formation, suggesting that this exopolysaccharide contributes to pellicle formation. Also associated with the pellicle matrix were three subunits of pili assembled by chaperon-usher systems: the major CsuA/B, A1S_1510 (presented 45% of identity with the main pilin F17-A from enterotoxigenic Escherichia coli pili) and A1S_2091. The presence of both PNAG polysaccharide and pili systems in matrix of pellicles might contribute to the virulence of this emerging pathogen.http://europepmc.org/articles/PMC4216135?pdf=render |
| spellingShingle | Yassine Nait Chabane Sara Marti Christophe Rihouey Stéphane Alexandre Julie Hardouin Olivier Lesouhaitier Jordi Vila Jeffrey B Kaplan Thierry Jouenne Emmanuelle Dé Characterisation of pellicles formed by Acinetobacter baumannii at the air-liquid interface. PLoS ONE |
| title | Characterisation of pellicles formed by Acinetobacter baumannii at the air-liquid interface. |
| title_full | Characterisation of pellicles formed by Acinetobacter baumannii at the air-liquid interface. |
| title_fullStr | Characterisation of pellicles formed by Acinetobacter baumannii at the air-liquid interface. |
| title_full_unstemmed | Characterisation of pellicles formed by Acinetobacter baumannii at the air-liquid interface. |
| title_short | Characterisation of pellicles formed by Acinetobacter baumannii at the air-liquid interface. |
| title_sort | characterisation of pellicles formed by acinetobacter baumannii at the air liquid interface |
| url | http://europepmc.org/articles/PMC4216135?pdf=render |
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