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                  <mods:namePart>Caro-Astorga, Joaquín</mods:namePart>
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                  <mods:namePart>Pérez-García, Alejandro</mods:namePart>
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                  <mods:namePart>De-Vicente-Moreno, Antonio</mods:namePart>
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                  <mods:namePart>Romero-Hinojosa, Diego Francisco</mods:namePart>
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                  <mods:dateAccessioned encoding="iso8601">2015-11-12T11:42:12Z</mods:dateAccessioned>
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               <mods:abstract>The formation of bacterial biofilms is a doable thanks to the assembly of an extracellular matrix that provides to the entire&#xd;
community with i) an outstanding architectonic structure and ii) protection to the cells from external aggressions. In&#xd;
Bacillus subtilis, a structural element dedicated to the formation of the extracellular matrix is the amyloid-like protein TasA.&#xd;
To form fibers, TasA needs the participation of the protein TapA. Indeed, a tapA mutant resembles phenotypically to a&#xd;
tasA mutant, which is wrinkle-less pellicles or colonies with no distinguishable morphological features. tasA is widely&#xd;
spread within the Bacillus genus, but tapA is absent in the heterogeneous group of Bacillus cereus which includes&#xd;
environmental and pathogenic members; some of them are responsible for important food intoxication outbreaks. Then,&#xd;
we asked whether TasA would still retain functionality in biofilm formation in B. cereus. Comparative genomic analysis&#xd;
showed a region in B. cereus containing two orthologous of tasA, tasA and calY, and the orthologous of sipW, that&#xd;
encodes a signal peptidase. Our mutagenic studies revealed that the entire region was relevant for biofilm formation, and&#xd;
electron microscopy proved the major propensity of TasA than CalY to form fibers in the cell surfaces. These findings also&#xd;
indicated that in B. cereus as opposed to B. subtilis, an accessory TapA protein is not necessary for the fibrillation of&#xd;
TasA. Indeed, the heterologous expression of this region of B. cereus restored the capacity of a B. subtilis tasA operon&#xd;
mutant or a single tasA mutant to form pellicles. These pellicles stained with the amyloid dye Congo Red and the cells&#xd;
were decorated with fibers, both findings suggestive of an amyloid-like nature of the B. cereus TasA. Intriguingly, in a B.&#xd;
subtilis tapA mutant, only the entire region of B. cereus fully rescued pellicle formation, fibrillation or Congo Red staining,&#xd;
to a lesser extent did sipw-tasA, and no restoration was observed with sipW-calY. These observations led us to speculate&#xd;
that TapA might cross seed the fibrillation of TasA or CalY in B. subtilis. In summary, TasA is relevant for biofilm formation&#xd;
in these two bacterial species, which appears to be governed by its polymerizing nature. The fact that we count with two&#xd;
bacterial species containing versions of TasA with subtle differences will be of great value in our studies of the&#xd;
mechanistic of polymerization of these bacterial amyloid-like fibers and their contribution to the assembly of the&#xd;
extracellular matrix.</mods:abstract>
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               <mods:subject>
                  <mods:topic>Biopelículas</mods:topic>
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               <mods:titleInfo>
                  <mods:title>A short version of the amyloid-like protein TasA fibrillates and supports biofilm formation in Bacillus cereus</mods:title>
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