Proteomic identification of CBM37-containing cellulases produced by the rumen cellulolytic bacterium <Emphasis Type="Italic">Ruminococcus albus</Emphasis> 20 and their putative involvement in bacterial adhesion to cellulose |
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Authors: | Harivony Rakotoarivonina Cécile Terrie Christophe Chambon Evelyne Forano Pascale Mosoni |
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Institution: | (1) INRA, UR454 Unité de Microbiologie, 63122 Saint-Genès-Champanelle, France;(2) INRA Plate Forme de Protéomique, 63122 Saint-Genès-Champanelle, France;(3) Present address: INRA, Université de Reims, FARE UMR614, 51688 Reims, France |
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Abstract: | The objective of this study was to identify and characterize other proteins than fimbrial proteins potentially involved in
R. albus 20 adhesion to cellulose using an adhesion-related antiserum preparation (i.e. anti-Adh serum). From protein fractions of
R. albus 20 grown on cellulose, the serum recognized at least 10 cellulose-binding proteins (CBPs), among which homologs of glycoside
hydrolases (family 5, 9 and 48) of R. albus 8 (i.e. Cel5G, Cel9B and Cel48A) were identified by a proteomic approach. In strain 20, Cel9B and Cel48A were identified
as two major CBPs and as bacterial cell-associated proteins. The anti-Adh serum was also shown to target the C-terminal family
37 carbohydrate-binding module (CBM37) of Cel9B and Cel48A, indicating that this module, unique to R. albus, may play a significant role in bacterial adhesion to cellulose as suggested previously for R. albus 8. Overall, our results support the hypothesis of an adhesion mechanism involving the CBM37 of Cel9B and Cel48A. This adhesion
mechanism may not be restricted to these two enzymes but may also involve other CBM37-containing proteins such as Cel5G and
the other uncharacterised proteins recognized by the anti-Adh serum.
The EMBL accession numbers for the sequences reported in this paper are FM872295 for Cel9B and FM872296 for Cel48A. |
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Keywords: | Ruminococcus albus Two-dimensional gel electrophoresis MALDI-TOF mass spectrometry Cellulolysis Adhesion |
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