The Listeria monocytogenes Sortase-B Recognizes Varied Amino Acids at Position 2 of the Sorting Motif

Mariscotti, Javier F.; Portillo, Francisco García‐del; Pucciarelli, M. Graciela

doi:10.1074/jbc.m807989200

Cited by 19 publications

(20 citation statements)

References 30 publications

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“…The D225A mutation may disrupt the active site architecture of SrtB, allowing recognition of various sequences as primary substrates, but it does not appear to play a direct role in the catalytic mechanism. Interestingly, similar promiscuous activity has been observed in several SrtA mutants (57, 58), as well as the wild-type SrtB enzyme from Listeria monocytogenes (59).…”

Section: Crystal Structure Of the Srtb-npqt* Complex And Computationamentioning

confidence: 68%

Structural and Computational Studies of the Staphylococcus aureus Sortase B-Substrate Complex Reveal a Substrate-stabilized Oxyanion Hole

Jacobitz

Wereszczynski

et al. 2014

Journal of Biological Chemistry

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Background: Sortase enzymes catalyze a transpeptidation reaction that displays bacterial surface proteins. Results: Structural and computational studies reveal how the sortase B enzyme recognizes its sorting signal substrate. Conclusion: Sortase enzymes catalyze transpeptidation using a substrate-stabilized oxyanion hole. Significance: The results of this work could facilitate the rational design of sortase inhibitors.

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Section: Crystal Structure Of the Srtb-npqt* Complex And Computationamentioning

confidence: 68%

Structural and Computational Studies of the Staphylococcus aureus Sortase B-Substrate Complex Reveal a Substrate-stabilized Oxyanion Hole

Jacobitz

Wereszczynski

et al. 2014

Journal of Biological Chemistry

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“…A subset of covalently attached cell wall proteins feature a different sorting motif, characterized by an NXXTX consensus sequence that targets surface protein precursors for sortase B processing (Comfort and Clubb, 2004; Mariscotti et al, 2009). Sortase B enzymes have few substrates, which are usually encoded by genes arranged in an operon together with srtB (Marraffini et al, 2006).…”

Section: Surface Protein Localization: Anchoring Domainsmentioning

confidence: 99%

“…One of them, SvpA, is a surface-associated protein required for iron uptake and bacterial persistence in mouse organs (Newton et al, 2005). The other listerial sortase B substrate, Lmo2186, possesses two putative sorting motifs, NKVT N and N PKSS (underlined residue is common to both), but only the latter is necessary for surface anchoring (Mariscotti et al, 2009). SvpA was first characterized as a virulence factor, as its depletion resulted in deficient escape from macrophage phagosomes (Borezée et al, 2001).…”

Section: Surface Protein Localization: Anchoring Domainsmentioning

confidence: 99%

How Listeria monocytogenes organizes its surface for virulence

Carvalho

Sousa

Cabanes

2014

Front. Cell. Infect. Microbiol.

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Listeria monocytogenes is a Gram-positive pathogen responsible for the manifestation of human listeriosis, an opportunistic foodborne disease with an associated high mortality rate. The key to the pathogenesis of listeriosis is the capacity of this bacterium to trigger its internalization by non-phagocytic cells and to survive and even replicate within phagocytes. The arsenal of virulence proteins deployed by L. monocytogenes to successfully promote the invasion and infection of host cells has been progressively unveiled over the past decades. A large majority of them is located at the cell envelope, which provides an interface for the establishment of close interactions between these bacterial factors and their host targets. Along the multistep pathways carrying these virulence proteins from the inner side of the cytoplasmic membrane to their cell envelope destination, a multiplicity of auxiliary proteins must act on the immature polypeptides to ensure that they not only maturate into fully functional effectors but also are placed or guided to their correct position in the bacterial surface. As the major scaffold for surface proteins, the cell wall and its metabolism are critical elements in listerial virulence. Conversely, the crucial physical support and protection provided by this structure make it an ideal target for the host immune system. Therefore, mechanisms involving fine modifications of cell envelope components are activated by L. monocytogenes to render it less recognizable by the innate immunity sensors or more resistant to the activity of antimicrobial effectors. This review provides a state-of-the-art compilation of the mechanisms used by L. monocytogenes to organize its surface for virulence, with special focus on those proteins that work “behind the frontline”, either supporting virulence effectors or ensuring the survival of the bacterium within its host.

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“…High resolution MS of the tryptic peptide mixture obtained from this material led to the unequivocal identification of 53 proteins (supplemental Table S1). The most abundant classes identified in this proteome included surface proteins covalently bound to peptidoglycan such as those bearing the LXPTG motif, the two sortase-B substrates Lmo2185 and Lmo2186 (34), and enzymes related to peptidoglycan metabolism (Table 1). A total of 15 LPXTG proteins covalently bound to the peptidoglycan were identified in the cell wall of intracellular bacteria (Table 1).…”

Section: Identification Of Surface Proteins In Cell Wall Of Intracellmentioning

confidence: 99%

Association of ActA to Peptidoglycan Revealed by Cell Wall Proteomics of Intracellular Listeria monocytogenes

Portillo

Calvo

D'Orazio

et al. 2011

Journal of Biological Chemistry

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Listeria monocytogenes is a Gram-positive intracellular bacterial pathogen that colonizes the cytosol of eukaryotic cells. Recent transcriptomic studies have revealed that intracellular L. monocytogenes alter expression of genes encoding envelope components. However, no comparative global analysis of this cell wall remodeling process is yet known at the protein level. Here, we used high resolution mass spectrometry to define the cell wall proteome of L. monocytogenes growing inside epithelial cells. When compared with extracellular bacteria growing in a nutrient-rich medium, a major difference found in the proteome was the presence of the actin assembly-inducing protein ActA in peptidoglycan purified from intracellular bacteria. ActA was also identified in the peptidoglycan of extracellular bacteria growing in a chemically defined minimal medium. In this condition, ActA maintains its membrane anchoring domain and promotes efficient bacterial entry into nonphagocytic host cells. Unexpectedly, Internalin-A, which mediates entry of extracellular L. monocytogenes into eukaryotic cells, was identified at late infection times (6 h) as an abundant protein in the cell wall of intracellular bacteria. Other surface proteins covalently bound to the peptidoglycan, as Lmo0514 and Lmo2085, were detected exclusively in intracellular and extracellular bacteria, respectively. Altogether, these data provide the first insights into the changes occurring at the protein level in the L. monocytogenes cell wall as the pathogen transits from the extracellular environment to an intracytosolic lifestyle inside eukaryotic cells. Some of these changes include alterations in the relative amount and the mode of association of certain surface proteins.

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The Listeria monocytogenes Sortase-B Recognizes Varied Amino Acids at Position 2 of the Sorting Motif

Cited by 19 publications

References 30 publications

Structural and Computational Studies of the Staphylococcus aureus Sortase B-Substrate Complex Reveal a Substrate-stabilized Oxyanion Hole

Structural and Computational Studies of the Staphylococcus aureus Sortase B-Substrate Complex Reveal a Substrate-stabilized Oxyanion Hole

How Listeria monocytogenes organizes its surface for virulence

Association of ActA to Peptidoglycan Revealed by Cell Wall Proteomics of Intracellular Listeria monocytogenes

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