Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus

Carneiro, Célia Regina Whitaker; Postol, Edilberto; Nomizo, Regina; Reis, Luiz F. L.; Brentani, Ricardo R.

doi:10.1016/j.micinf.2004.02.003

Cited by 128 publications

(56 citation statements)

References 19 publications

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“…Such “moonlighting” functions of proteins appear to be widespread. In particular, enzymes of glycolysis are commonly observed associating with the cell surface and mediating host factor attachment (26–28). For example, GAPDH and enolase were found to associate, at low pH, with the cell surface of L. crispatus cells and to mediate host attachment (29).…”

Section: Discussionmentioning

confidence: 99%

The Extracellular Matrix of Staphylococcus aureus Biofilms Comprises Cytoplasmic Proteins That Associate with the Cell Surface in Response to Decreasing pH

Foulston

Elsholz

DeFrancesco

et al. 2014

mBio

174

178

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Biofilm formation by Staphylococcus aureus involves the formation of an extracellular matrix, but the composition of this matrix has been uncertain. Here we report that the matrix is largely composed of cytoplasmic proteins that reversibly associate with the cell surface in a manner that depends on pH. We propose a model for biofilm formation in which cytoplasmic proteins are released from cells in stationary phase. These proteins associate with the cell surface in response to decreasing pH during biofilm formation. Rather than utilizing a dedicated matrix protein, S. aureus appears to recycle cytoplasmic proteins that moonlight as components of the extracellular matrix.

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Section: Discussionmentioning

confidence: 99%

The Extracellular Matrix of Staphylococcus aureus Biofilms Comprises Cytoplasmic Proteins That Associate with the Cell Surface in Response to Decreasing pH

Foulston

Elsholz

DeFrancesco

et al. 2014

mBio

174

178

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“…Several pathogenic species seem to retain moonlighting proteins on cell surface at neutral pH [38,39,41,42,45,50,53,60], whereas this is not the case for several lactobacilli [16,28,32,47,92]. The latter is illustrated for L. crispatus in Figure 3.…”

Section: Discussionmentioning

confidence: 99%

Dancing to Another Tune—Adhesive Moonlighting Proteins in Bacteria

Kainulainen

Korhonen

2014

Biology

128

136

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Biological moonlighting refers to proteins which express more than one function. Moonlighting proteins occur in pathogenic and commensal as well as in Gram-positive and Gram-negative bacteria. The canonical functions of moonlighting proteins are in essential cellular processes, i.e., glycolysis, protein synthesis, chaperone activity, and nucleic acid stability, and their moonlighting functions include binding to host epithelial and phagocytic cells, subepithelia, cytoskeleton as well as to mucins and circulating proteins of the immune and hemostatic systems. Sequences of the moonlighting proteins do not contain known motifs for surface export or anchoring, and it has remained open whether bacterial moonlighting proteins are actively secreted to the cell wall or whether they are released from traumatized cells and then rebind onto the bacteria. In lactobacilli, ionic interactions with lipoteichoic acids and with cell division sites are important for surface localization of the proteins. Moonlighting proteins represent an abundant class of bacterial adhesins that are part of bacterial interactions with the environment and in responses to environmental changes. Multifunctionality in bacterial surface proteins appears common: the canonical adhesion proteins fimbriae express also nonadhesive functions, whereas the mobility organelles flagella as well as surface proteases express adhesive functions.

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“…It is important to point out that some of these proteins that we classified as cytoplasmic proteins by different web-server predictors (e.g. enolase, Inosine-5′-monophosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, pyruvate dehydrogenase, triosephosphate isomerase, elongation factor Tu, and GroEL) have been described as “moonlight proteins” since they perform more than one function on the cell [56], [57] and have been identified on the cell surface of some gram-positive bacterial pathogens [33], [58]–[67]. Although the proteins mentioned above are predicted to be cytoplasmic we cannot be ruled out their possible surface location and should be consider as good candidates for further immunological studies.…”

Section: Discussionmentioning

confidence: 99%

Identification of Peptidoglycan-Associated Proteins as Vaccine Candidates for Enterococcal Infections

et al. 2014

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Infections by opportunistic bacteria have significant contributions to morbidity and mortality of hospitalized patients and also lead to high expenses in healthcare. In this setting, one of the major clinical problems is caused by Gram-positive bacteria such as enterococci and staphylococci. In this study we extract, purify, identify and characterize immunogenic surface-exposed proteins present in the vancomycin resistant enterococci (VRE) strain Enterococcus faecium E155 using three different extraction methods: trypsin shaving, biotinylation and elution at high pH. Proteomic profiling was carried out by gel-free and gel-nanoLC-MS/MS analyses. The total proteins found with each method were 390 by the trypsin shaving, 329 by the elution at high pH, and 45 using biotinylation. An exclusively extracytoplasmic localization was predicted in 39 (10%) by trypsin shaving, in 47 (15%) by elution at high pH, and 27 (63%) by biotinylation. Comparison between the three extraction methods by Venn diagram and subcellular localization predictors (CELLO v.2.5 and Gpos-mPLoc) allowed us to identify six proteins that are most likely surface-exposed: the SCP-like extracellular protein, a low affinity penicillin-binding protein 5 (PBP5), a basic membrane lipoprotein, a peptidoglycan-binding protein LysM (LysM), a D-alanyl-D-alanine carboxypeptidase (DdcP) and the peptidyl-prolyl cis-trans isomerase (PpiC). Due to their close relationship with the peptidoglycan, we chose PBP5, LysM, DdcP and PpiC to test their potential as vaccine candidates. These putative surface-exposed proteins were overexpressed in Escherichia coli and purified. Rabbit polyclonal antibodies raised against the purified proteins were able to induce specific opsonic antibodies that mediated killing of the homologous strain E. faecium E155 as well as clinical strains E. faecium E1162, Enterococcus faecalis 12030, type 2 and type 5. Passive immunization with rabbit antibodies raised against these proteins reduced significantly the colony counts of E. faecium E155 in mice, indicating the effectiveness of these surface-related proteins as promising vaccine candidates to target different enterococcal pathogens.

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Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus

Cited by 128 publications

References 19 publications

The Extracellular Matrix of Staphylococcus aureus Biofilms Comprises Cytoplasmic Proteins That Associate with the Cell Surface in Response to Decreasing pH

The Extracellular Matrix of Staphylococcus aureus Biofilms Comprises Cytoplasmic Proteins That Associate with the Cell Surface in Response to Decreasing pH

Dancing to Another Tune—Adhesive Moonlighting Proteins in Bacteria

Identification of Peptidoglycan-Associated Proteins as Vaccine Candidates for Enterococcal Infections

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