A comparative study ofBacillus cereus,Bacillus thuringiensis andBacillus anthracis extracellular proteomes

Gohar, Michel; Gilois, Nathalie; Graveline, Richard; Garreau, Christelle; Sanchis, Vincent; Lereclus, Didier

doi:10.1002/pmic.200401225

Cited by 111 publications

(100 citation statements)

References 63 publications

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“…One can assume that under nondividing conditions, a halt in LTA synthesis is essential for bacteria to maintain a normal membrane composition and integrity. The proteolytic cleavage of LtaS-type enzymes appears to be a more general phenomenon for this class of proteins, as processed forms have now been detected in a range of Gram-positive bacteria (2,18,23,37,44). Our findings, combined with the results of previously published studies (1,37), provide more and more evidence that this processing step is performed by type I signal peptidases.…”

Section: Discussionsupporting

confidence: 77%

“…Similarly, processed forms of LtaS-type enzymes were found in the supernatants of L. monocytogenes, Bacillus anthracis, Bacillus cereus, Bacillus thuringiensis, and Staphylococcus epidermidis cultures (2,18,37,44). In all cases where the cleavage site of LtaS-type enzymes has been mapped, it occurs after an Ala-X-Ala motif, and the location of the motif within the protein is conserved in LtaStype enzymes.…”

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confidence: 96%

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Proteolytic Cleavage Inactivates the Staphylococcus aureus Lipoteichoic Acid Synthase

et al. 2011

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Lipoteichoic acid (LTA) is a crucial cell envelope component in Gram-positive bacteria. In Staphylococcus aureus, the polyglycerolphosphate LTA molecule is synthesized by LtaS, a membrane-embedded enzyme with five N-terminal transmembrane helices (5TM domain) that are connected via a linker region to the C-terminal extracellular enzymatic domain (eLtaS). The LtaS enzyme is processed during bacterial growth, and the eLtaS domain is released from the bacterial membrane. Here we provide experimental evidence that the proteolytic cleavage following residues 215 Ala-Leu-Ala 217 is performed by the essential S. aureus signal peptidase SpsB, as depletion of spsB results in reduced LtaS processing. In addition, the introduction of a proline residue at the ؉1 position with respect to the cleavage site, a substitution known to inhibit signal peptidase-dependent cleavage, abolished LtaS processing at this site. It was further shown that the 5TM domain is crucial for enzyme function. The observation that the construction of hybrid proteins between two functional LtaS-type enzymes resulted in the production of proteins unable to synthesize LTA suggests that specific interactions between the 5TM and eLtaS domains are required for function. No enzyme activity was detected upon expression of the 5TM and eLtaS domains as separate fragments, indicating that the two domains cannot assemble postsynthesis to form a functional enzyme. Taken together, our data suggest that only the full-length LtaS enzyme is active in the LTA synthesis pathway and that the proteolytic cleavage step is used as a mechanism to irreversibly inactivate the enzyme.

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Section: Discussionsupporting

confidence: 77%

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confidence: 96%

Proteolytic Cleavage Inactivates the Staphylococcus aureus Lipoteichoic Acid Synthase

et al. 2011

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“…En términos de diversidad, la familia Enterobacteriacae presentó 10 especies, seguida por Bacillaceae (6) y Streptococcaceae (4). A nivel de cepas, las bacterias cultivables más aisladas fueron P. aeruginosa (40), S. aureus (16), Pseudomonas sp (15), Klebsiella oxytoca (4). Otros microorganismos que incluían a familias como Enterobacteriaceae y Bacillaceae se presentaron en menores cantidades (Tabla 1).…”

Section: Resultsunclassified

“…Estudios comparativos entre B. cereus, B. thuringiensis, y B. anthracis han mostrado que sus proteínas de la pared celular y del citosol son muy similares entre sí, (40) resaltando que estas especies comparten un fondo genético similar. Estos autores identificaron las proteínas citosólicas: enolasa, GroEl, entre otras.…”

Section: Discussionunclassified

Caracterización molecular de bacterias patógenas de las vías respiratorias de pacientes peruanos con fibrosis quística

Aquino

Gonzáles

Samaniego³

et al. 2017

Rev Peru Med Exp Salud Publica

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“…In addition, SCWPs bind SLH (S-layer homology) domains containing proteins, thus anchoring them non-covalently to the cell wall (3). These proteins are involved in various functions, including peptidoglycan maturation (4,5), binding to host tissues (6), or protein degradation (7). Teichoic acids and the secondary cell wall polysaccharide were also reported to be involved in biofilm formation (8 -10).…”

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confidence: 99%

Environmental and Biofilm-dependent Changes in a Bacillus cereus Secondary Cell Wall Polysaccharide

Candela

Maës

Garenáux

et al. 2011

Journal of Biological Chemistry

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Bacterial species from the Bacillus genus, including Bacillus cereus and Bacillus anthracis, synthesize secondary cell wall polymers (SCWP) covalently associated to the peptidoglycan through a phospho-diester linkage. Although such components were observed in a wide panel of B. cereus and B. anthracis strains, the effect of culture conditions or of bacterial growth state on their synthesis has never been addressed. Herein we show that B. cereus ATCC 14579 can synthesize not only one, as previously reported, but two structurally unrelated secondary cell wall polymers (SCWP) polysaccharides. The first of these SCWP, 34)[GlcNAc(␤1-3)]GlcNAc(␤1-6)[Glc(␤1-3)][ManNAc(␣1-4)]GalNAc(␣1-4)ManNAc(␤13, although presenting an original sequence, fits to the already described the canonical sequence motif of SCWP. In contrast, the second polysaccharide was made up by a totally original sequence, 36)-Gal(␣1-2)(2-R-hydroxyglutar-5-ylamido)Fuc2NAc4N(␣1-6)GlcNAc(␤13, which no equivalent has ever been identified in the Bacillus genus. In addition, we established that the syntheses of these two polysaccharides were differently regulated. The first one is constantly expressed at the surface of the bacteria, whereas the expression of the second is tightly regulated by culture conditions and growth states, planktonic, or biofilm.The cell wall surrounding cytoplasmic membrane is of prime importance in bacteria survival and adaptation to their environment. In Gram-positive bacteria, the cell wall includes a thick multilayer peptidoglycan to which most often are associated other cell-surface structures called secondary cell wall polymers (SCWPs) 4 (1). These secondary cell wall polymers include lipoteichoic acids anchored in the outer leaflet of plasmic membrane as well as teichoic acids, teichuronic acids, or neutral polysaccharides (SCWP polysaccharides), which are covalently bound, through a phosphodiester link, to the N-acetyl muramic acid moieties of the peptidoglycan. SCWPs are essential in Bacillus subtilis and were shown to be involved in the bacterial virulence in Staphylococcus aureus (2). In addition, SCWPs bind SLH (S-layer homology) domains containing proteins, thus anchoring them non-covalently to the cell wall (3). These proteins are involved in various functions, including peptidoglycan maturation (4, 5), binding to host tissues (6), or protein degradation (7). Teichoic acids and the secondary cell wall polysaccharide were also reported to be involved in biofilm formation (8 -10).Biofilms are multicellular structures attached to a solid or a liquid surface and embedded in a self-produced matrix. This matrix is made of polymers, mostly polysaccharides, DNA, and/or proteins, provides cohesion to the bacterial community (11-13), and acts as a shield, protecting bacteria within the biofilm. Biofilms are, therefore, persistent structures, resisting desiccation, cleaning procedures, and antimicrobial substances (14), which makes them a challenge in human health and industrial processes. Several species from the Bacillus genus, in...

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A comparative study ofBacillus cereus,Bacillus thuringiensis andBacillus anthracis extracellular proteomes

Cited by 111 publications

References 63 publications

Proteolytic Cleavage Inactivates the Staphylococcus aureus Lipoteichoic Acid Synthase

Proteolytic Cleavage Inactivates the Staphylococcus aureus Lipoteichoic Acid Synthase

Caracterización molecular de bacterias patógenas de las vías respiratorias de pacientes peruanos con fibrosis quística

Environmental and Biofilm-dependent Changes in a Bacillus cereus Secondary Cell Wall Polysaccharide

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