Anchoring of LPXTG-Like Proteins to the Gram-Positive Cell Wall Envelope

Siegel, Sara D.; Reardon, Melissa E.; Ton‐That, Hung

doi:10.1007/82_2016_8

Cited by 35 publications

(33 citation statements)

References 92 publications

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“…The precursor form of these proteins contains a signal peptide and a C-terminal cell wall sorting signal (CWSS), which is comprised of a LPXTG motif, followed by a hydrophobic domain and a short tail of positively charged residues [18]. The CWSS is necessary and sufficient for cell wall attachment mediated by a conserved transpeptidase enzyme named sortase SrtA first discovered in S. aureus [19,20].…”

Section: Attaching Surface Proteins and Pilus Polymers To The Bacterimentioning

confidence: 99%

“…The CWSS is necessary and sufficient for cell wall attachment mediated by a conserved transpeptidase enzyme named sortase SrtA first discovered in S. aureus [19,20]. Results from structural studies and in vivo studies of SrtA [21,22], as well as in vitro reconstitution of cell wall anchoring [22,23], put forth a well-known model of sortase-catalyzed cell wall anchoring of surface proteins [18,24,25], whereby the membrane-bound sortase SrtA enzyme cleaves the LPXTG motif between threonine and glycine and links the cleaved substrate to the amino-group of the pentaglycyl cross-bridge within lipid II; the generated product is ultimately incorporated into the cell wall. The enzymatic activity of sortase requires two conserved residues Cys and His [26], which constitute a catalytic pocket within the β-barrel structure of SrtA [21].…”

Section: Attaching Surface Proteins and Pilus Polymers To The Bacterimentioning

confidence: 99%

“…They are the only sortase enzymes that have polymerizing activities or pilus polymerization, i.e. linking monomeric proteins into covalently bonded polymers, hence called pilus-specific sortase [18,27]. Sortase-mediated pilus polymerization was first described in C. diphtheriae with the SpaA pilus, which is comprised of the pilus shaft SpaA, pilus tip SpaC and pilus base SpaB, with all pilins containing the CWSS [34].…”

Section: Attaching Surface Proteins and Pilus Polymers To The Bacterimentioning

confidence: 99%

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Biogenesis of the Gram-positive bacterial cell envelope

Siegel

Ton‐That

2016

Current Opinion in Microbiology

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The Gram-positive cell envelope serves as a molecular platform for surface display of capsular polysaccharides, wall teichoic acids (WTAs), lipoteichoic acids (LTAs), lipoproteins, surface proteins and pili. WTAs, LTAs, and sortase-assembled pili are a few features that make the Gram-positive cell envelope distinct from the Gram-negative counterpart. Interestingly, a set of LytR-CpsA-Psr family proteins, found in all Gram-positives but limited to a minority of Gram-negative organisms, plays divergent functions, while decorating the cell envelope with glycans. Furthermore, a phylum of Gram-positive bacteria, the actinobacteria, appear to employ oxidative protein folding as the major folding mechanism, typically occurring in an oxidizing environment of the Gram-negative periplasm. These distinctive features will be highlighted, along with recent findings in the cell envelope biogenesis.

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Section: Attaching Surface Proteins and Pilus Polymers To The Bacterimentioning

confidence: 99%

Section: Attaching Surface Proteins and Pilus Polymers To The Bacterimentioning

confidence: 99%

Section: Attaching Surface Proteins and Pilus Polymers To The Bacterimentioning

confidence: 99%

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Biogenesis of the Gram-positive bacterial cell envelope

Siegel

Ton‐That

2016

Current Opinion in Microbiology

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“…LPXTG-containing proteins are cell surface proteins covalently linked to the peptidoglycan through the action of sortase enzymes. These proteins are known to fulfill functions mainly linked to the interactions of pathogenic strains with their host (17). Thus, it is not surprising that only rare S. thermophilus strains harbor LPXTG proteins at their surface (14).…”

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confidence: 99%

Impact of Cell Surface Molecules on Conjugative Transfer of the Integrative and Conjugative Element ICE St3 of Streptococcus thermophilus

Dahmane

Robert

Deschamps

et al. 2018

Appl Environ Microbiol

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Integrative conjugative elements (ICEs) are chromosomal elements that are widely distributed in bacterial genomes, hence contributing to genome plasticity, adaptation, and evolution of bacteria. Conjugation requires a contact between both the donor and the recipient cells and thus likely depends on the composition of the cell surface envelope. In this work, we investigated the impact of different cell surface molecules, including cell surface proteins, wall teichoic acids, lipoteichoic acids, and exopolysaccharides, on the transfer and acquisition of ICE from The transfer of ICE from wild-type (WT) donor cells to mutated recipient cells increased 5- to 400-fold when recipient cells were affected in lipoproteins, teichoic acids, or exopolysaccharides compared to when the recipient cells were WT. These mutants displayed an increased biofilm-forming ability compared to the WT, suggesting better cell interactions that could contribute to the increase of ICE acquisition. Microscopic observations of cell surface mutants showed different phenotypes (aggregation in particular) that can also have an impact on conjugation. In contrast, the same mutations did not have the same impact when the donor cells, instead of recipient cells, were mutated. In that case, the transfer frequency of ICE decreased compared to that with the WT. The same observation was made when both donor and recipient cells were mutated. The dominant effect of mutations in donor cells suggests that modifications of the cell envelope could impair the establishment or activity of the conjugation machinery required for DNA transport. ICEs contribute to horizontal gene transfer of adaptive traits (for example, virulence, antibiotic resistance, or biofilm formation) and play a considerable role in bacterial genome evolution, thus underlining the need of a better understanding of their conjugative mechanism of transfer. While most studies focus on the different functions encoded by ICEs, little is known about the effect of host factors on their conjugative transfer. Using ICE of as a model, we demonstrated the impact of lipoproteins, teichoic acids, and exopolysaccharides on ICE transfer and acquisition. This opens up new avenues to control gene transfer mediated by ICEs.

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“…Therefore, in this study, we investigated four of ST-261 adhesins, one that is specific to serotype Ib piscine strains and three that are conserved among all strains, in order to assess if they would be good candidate antigens for the development of a crossprotective vaccine against multiple serotypes. All the identified ST-261 adhesins display a signal peptide sequence at the N-terminus and a LPXTG anchor motif at the C-terminal suggesting that they are cell-wall anchored proteins (Novick, 2000;Schneewind and Missiakas, 2012;Siegel et al, 2017). Two ST-261 adhesins, adhesin_0337 and 0626, exhibit domain repeats in their amino acid sequences, characteristic of adhesins in streptococci (Nobbs et al, 2015).…”

Section: Changes In the Protein Profile Of Qma0285 Cultured In Differmentioning

confidence: 99%

A pan genome reverse vaccinology approach to prevent Streptococcus agalactiae infection in farmed tilapia

Kawasaki¹

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Streptococcus agalactiae (Group B Streptococcus; GBS) is a Gram-positive pathogenic bacterium that causes disease in a wide range of animals including fish. Outbreaks of GBS in farmed fish have substantial economic impacts on the aquaculture industry, especially in tilapia production, a staple food product in tropical and subtropical low-and middle-income countries and the second most widely farmed fish after carp. Although vaccination can effectively prevent disease caused by GBS in fish it often fails after relatively short periods of use. Capsular polysaccharide (CPS) is the major protective antigen in GBS vaccines and a critical virulence factor. There are currently ten CPS serotypes of GBS and, whilst vaccination against one serotype confers protection in fish, it is not cross-protective against other serotypes. In addition, under the strong selective pressure of vaccination-driven adaptive immunity, evolution of novel serotypes can occur. To improve the serotype crossprotective efficacy of GBS vaccines for aquaculture, I employed a pan-genome reverse vaccinology approach to design candidate serotype-independent protective vaccines based on conserved proteins in fish-pathogenic GBS serotypes. Reverse vaccinology exploits recent advances in genomics to predict antigens in the genome sequence. Reverse vaccinology combined with pan-genome can identify the antigens that are conserved across a diversity of strains of a pathogen.To identify potential vaccine candidate antigens, a pan-genome was constructed for GBS comprising 82 genomes including representative isolates from wild marine fish and stingrays, farm and companion animals and from human clinical cases in Australia, along with isolates from farmed tilapia in Honduras and representative genomes from all current serotypes available via the NCBI Genbank database. Core genome single nucleotide polymorphism 3 (SNP) analysis indicated dissemination of the aquatic host-adapted ST-261 lineage in wild Australian fish from an ancestral tilapia strain, which is congruent with several introductions of tilapia into northern Australia from Israel and Malaysia during the 1970s and 1980s.Aquatic serotype Ib GBS strains have lost many virulence factors during adaptation, but six adhesins, named ST-261 adhesins, were well-conserved across the aquatic isolates and might be critical for virulence in fish and good targets for vaccine development. Three of six ST-261 adhesins were also conserved across all strains including terrestrial isolates and were chosen as vaccine candidates. Expressions of ST-261 adhesin genes were inversely co-regulated with CPS expression dependent upon carbon source and metal ions in the medium. However, gene transcription was not reflective of surface expression as serum antibodies derived in tilapia against recombinant adhesins did not detect similar variation in the level of ST-261 adhesins in whole cell ELISA or Western blot. This may be due to posttranscriptional processing causing a disconnect between gene and protein expression.To evaluate th...

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Anchoring of LPXTG-Like Proteins to the Gram-Positive Cell Wall Envelope

Cited by 35 publications

References 92 publications

Biogenesis of the Gram-positive bacterial cell envelope

Biogenesis of the Gram-positive bacterial cell envelope

Impact of Cell Surface Molecules on Conjugative Transfer of the Integrative and Conjugative Element ICE St3 of Streptococcus thermophilus

A pan genome reverse vaccinology approach to prevent Streptococcus agalactiae infection in farmed tilapia

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