The E1 beta-subunit of pyruvate dehydrogenase is surface-expressed in Lactobacillus plantarum and binds fibronectin

Vastano, Valeria; Salzillo, Marzia; Siciliano, Rosa Anna; Muscariello, Lidia; Sacco, Margherita; Marasco, Rosangela

doi:10.1016/j.micres.2013.07.013

Cited by 29 publications

(27 citation statements)

References 42 publications

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“…Antibodies specific to PdhA, PdhB, and PdhC were detected in sera of animals infected with M. bovis (45). PdhB was shown to be surface localized in Lactobacillus plantarum and interacts with human fibronectin (46). Tkt was found to be antigenic among membraneassociated proteins of Mycoplasma mycoides subsp.…”

Section: Discussionmentioning

confidence: 99%

Network of Surface-Displayed Glycolytic Enzymes in Mycoplasma pneumoniae and Their Interactions with Human Plasminogen

et al. 2016

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In different bacteria, primarily cytosolic and metabolic proteins are characterized as surface localized and interacting with different host factors. These moonlighting proteins include glycolytic enzymes, and it has been hypothesized that they influence the virulence of pathogenic species. The presence of surface-displayed glycolytic enzymes and their interaction with human plasminogen as an important host factor were investigated in the genome-reduced and cell wall-less microorganism Mycoplasma pneumoniae, a common agent of respiratory tract infections of humans. After successful expression of 19 glycolytic enzymes and production of polyclonal antisera, the localization of proteins in the mycoplasma cell was characterized using fractionation of total proteins, colony blot, mild proteolysis and immunofluorescence of M. pneumoniae cells. Eight glycolytic enzymes, pyruvate dehydrogenases A to C (PdhA-C), glyceraldehyde-3-phosphate dehydrogenase (GapA), lactate dehydrogenase (Ldh), phosphoglycerate mutase (Pgm), pyruvate kinase (Pyk), and transketolase (Tkt), were confirmed as surface expressed and all are able to interact with plasminogen. Plasminogen bound to recombinant proteins PdhB, GapA, and Pyk was converted to plasmin in the presence of urokinase plasminogen activator and plasmin-specific substrate D-valyl-leucyl-lysine-p-nitroanilide dihydrochloride. Furthermore, human fibrinogen was degraded by the complex of plasminogen and recombinant protein PdhB or Pgm. In addition, surface-displayed proteins (except PdhC) bind to human lung epithelial cells, and the interaction was reduced significantly by preincubation of cells with antiplasminogen. Our results suggest that plasminogen binding and activation by different surface-localized glycolytic enzymes of M. pneumoniae may play a role in successful and long-term colonization of the human respiratory tract. Members of the class Mollicutes are known to be the smallest and simplest self-replicating prokaryotes. Among them, Mycoplasma pneumoniae is a common pathogen in humans. The cell wall-less bacterium causes infections of the respiratory tract, including severe interstitial pneumonia (1), and usually accounts for 5 to 10% of all cases of community-acquired pneumonia among pediatric (2) and adult (3) patients. Because of the timedependent incidence of infections, Ͼ25% of pneumonia cases in epidemic periods are attributed to this agent (4). In addition, a number of extrapulmonary manifestations and complications are described, affecting mainly the skin and the central nervous system (5).Due to the greatly reduced genome of M. pneumoniae (816 kbp, 689 open reading frames [ORFs]), the metabolic pathways and the repertoire of virulence factors are limited (6). However, M. pneumoniae has developed effective strategies to infect humans and allow long-term survival in the respiratory mucosa. These include the targeted adherence of the bacteria to epithelial cells via a specialized complex of adhesins and adhesion-related proteins (7) as the first step in colonization,...

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Section: Discussionmentioning

confidence: 99%

Network of Surface-Displayed Glycolytic Enzymes in Mycoplasma pneumoniae and Their Interactions with Human Plasminogen

et al. 2016

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“…The adherence of bacteria via adhesins (bacterial lectins) to host mucins and matrix proteins of the intestine is a crucial step in the colonization process of pathogens such as Streptococcus, Staphylococcus, Mycobacterium, Borrelia, Listeria, Clostridium and Campylobacter [36,37]. Therefore, milk from secretor mothers has an advantage in protecting against diarrhea, because α1,2-fucosylated glycans may act as inhibitors of Campylobacter and calicivirus colonization [32].…”

Section: Discussionmentioning

confidence: 99%

Terminal glycotope expression on milk fibronectin differs from plasma fibronectin and changes over lactation

Orczyk-Pawiłowicz

Hirnle

Berghausen-Mazur

et al. 2015

Clinical Biochemistry

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“…In this context, commensal or probiotic bacteria capable of adhering ECM may compete with pathogens to colonize on the host surface, and hence prevent their invasion further deep into the tissue. 37 Indeed, commensal and pathogenic bacteria express several cell surface moonlighting proteins in common that bind to the ECM glycoproteins, e.g., enolase, 38,39 glyceraldehyde-3-phosphate dehydrogenase, 39,40 and pyruvate dehydrogenase, 41,42 supporting possibly the feasibility of so-called "competitive exclusion".…”

mentioning

confidence: 99%

Is it feasible to control pathogen infection by competitive binding of probiotics to the host?

Fukuda

2017

Virulence

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The E1 beta-subunit of pyruvate dehydrogenase is surface-expressed in Lactobacillus plantarum and binds fibronectin

Cited by 29 publications

References 42 publications

Network of Surface-Displayed Glycolytic Enzymes in Mycoplasma pneumoniae and Their Interactions with Human Plasminogen

Network of Surface-Displayed Glycolytic Enzymes in Mycoplasma pneumoniae and Their Interactions with Human Plasminogen

Terminal glycotope expression on milk fibronectin differs from plasma fibronectin and changes over lactation

Is it feasible to control pathogen infection by competitive binding of probiotics to the host?

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