Fibrinogen binds to nontoxigenic and toxigenic Corynebacterium diphtheriae strains

Sabbadini, Priscila Soares; Genovez, Marcia Rocha Novais; Silva, Cecília Ferreira da; Adelino, Thelma Lúcia Novaes; Santos, Cíntia Silva; Pereira, Geraldo; Nagao, Prescilla Emy; Dias, Alexandre de Souza de Oliveira Alves; Mattos‐Guaraldi, Ana Luíza; Júnior, Raphael Hirata

doi:10.1590/s0074-02762010000500018

Cited by 20 publications

(13 citation statements)

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“…Fbg and fibrin play overlapping roles in blood clotting, fibrinolysis, the inflammatory response, cellular and matrix interactions and wound healing ( Mosesson 2005 ). The Fbg binding properties of Staphylococcus aureus ( O’Neill et al 2008 ), Streptococcus suis ( Bonifait et al 2008 ) and C. diphtheriae ( Gomes et al 2009 , Sabbadini et al 2010 ) allow them to attach to each other through Fbg-mediated cross-bridging, contributing to biofilm production. The ability of C. striatum strains to bind to Fbg was also demonstrated in the present study.…”

Section: Discussionmentioning

confidence: 99%

Biofilm production by multiresistant Corynebacterium striatumassociated with nosocomial outbreak

Souza

Faria

Sant’Anna

et al. 2015

Mem. Inst. Oswaldo Cruz

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Corynebacterium striatum is a potentially pathogenic microorganism that causes nosocomial outbreaks. However, little is known about its virulence factors that may contribute to healthcare-associated infections (HAIs). We investigated the biofilm production on abiotic surfaces of multidrug-resistant (MDR) and multidrug-susceptible (MDS) strains of C. striatum of pulsed-field gel electrophoresis types I-MDR, II-MDR, III-MDS and IV-MDS isolated during a nosocomial outbreak in Rio de Janeiro, Brazil. The results showed that C. striatum was able to adhere to hydrophilic and hydrophobic abiotic surfaces. The C. striatum 1987/I-MDR strain, predominantly isolated from patients undergoing endotracheal intubation procedures, showed the greatest ability to adhere to all surfaces. C. striatum bound fibrinogen to its surface, which contributed to biofilm formation. Scanning electron microscopy showed the production of mature biofilms on polyurethane catheters by all pulsotypes. In conclusion, biofilm production may contribute to the establishment of HAIs caused by C. striatum.

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Section: Discussionmentioning

confidence: 99%

Biofilm production by multiresistant Corynebacterium striatumassociated with nosocomial outbreak

Souza

Faria

Sant’Anna

et al. 2015

Mem. Inst. Oswaldo Cruz

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“…Many pathogens colonize human tissues or evade immune mechanisms of bacterial clearance exploiting extracellular matrix and/or plasma proteins to colonize human tissues or to evade immune mechanisms for clearance of bacteria (Simpson-Louredo et al, 2014). Sabbadini et al (2010) suggested that the conversion of fibrinogen to fibrin may be connected to pseudomembrane formation, since differences in the abilities to bind and convert fibrinogen may partially explain differences in the extent of pseudomembrane formation during diphtheria. Obviously, DIP0733 is involved in these processes, but is not exclusively responsible for binding.…”

Section: Discussionmentioning

confidence: 99%

“…Sabbadini et al (2010) already demonstrated that Cor. diphtheriae is able to bind to fibrinogen and convert it to fibrin.…”

Section: Binding To Extracellular Matrix Proteins and Fibrinogenmentioning

confidence: 95%

Characterization of DIP0733, a multi-functional virulence factor of Corynebacterium diphtheriae

et al. 2015

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Corynebacterium diphtheriae is typically recognized as an extracellular pathogen. However, a number of studies revealed its ability to invade epithelial cells, indicating a more complex pathogen-host interaction. The molecular mechanisms controlling and facilitating internalization of Cor. diphtheriae are poorly understood. In this study, we investigated the role of DIP0733 as virulence factor to elucidate how it contributes to the process of pathogen-host cell interaction. Based on in vitro experiments, it was suggested recently that the DIP0733 protein might be involved in adhesion, invasion of epithelial cells and induction of apoptosis. A corresponding Cor. diphtheriae mutant strain generated in this study was attenuated in its ability to colonize and kill the host in a Caenorhabditis elegans infection model system. Furthermore, the mutant showed an altered adhesion pattern and a drastically reduced ability to adhere and invade epithelial cells. Subsequent experiments showed an influence of DIP0733 on binding of Cor. diphtheriae to extracellular matrix proteins such as collagen and fibronectin. Furthermore, based on its fibrinogen-binding activity, DIP0733 may play a role in avoiding recognition of Cor. diphtheriae by the immune system. In summary, our findings support the idea that DIP0733 is a multi-functional virulence factor of Cor. diphtheriae.

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“…In previous studies, the interaction of C. diphtheriae with proteins of the extracellular matrix surrounding eukaryotic cells, e. g. collagen I and IV, was reported [12, 14, 19, 27]. Additionally, the interaction with fibrinogen, a major component of the human plasma, which is crucial for blood clot formation due to its conversion into insoluble fibrin, has also been investigated in corynebacteria [27–29].…”

Section: Resultsmentioning

confidence: 99%

“…Additionally, the interaction with fibrinogen, a major component of the human plasma, which is crucial for blood clot formation due to its conversion into insoluble fibrin, has also been investigated in corynebacteria [27–29]. …”

Section: Resultsmentioning

confidence: 99%

The C-terminal coiled-coil domain of Corynebacterium diphtheriae DIP0733 is crucial for interaction with epithelial cells and pathogenicity in invertebrate animal model systems

et al. 2018

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BackgroundCorynebacterium diphtheriae is the etiologic agent of diphtheria and different systemic infections. The bacterium has been classically described as an extracellular pathogen. However, a number of studies revealed its ability to invade epithelial cells, indicating a more complex pathogen-host interaction. The molecular mechanisms controlling and facilitating internalization of C. diphtheriae still remains unclear. Recently, the DIP0733 transmembrane protein was found to play an important role in the interaction with matrix proteins and cell surfaces, nematode colonization, cellular internalization and induction of cell death.ResultsIn this study, we identified a number of short linear motifs and structural elements of DIP0733 with putative importance in virulence, using bioinformatic approaches. A C-terminal coiled-coil region of the protein was considered particularly important, since it was found only in DIP0733 homologs in pathogenic Corynebacterium species but not in non-pathogenic corynebacteria. Infections of epithelial cells and transepithelial resistance assays revealed that bacteria expressing the truncated form of C. diphtheriae DIP0733 and C. glutamicum DIP0733 homolog are less virulent, while the fusion of the coiled-coil sequence to the DIP0733 homolog from C. glutamicum resulted in increased pathogenicity. These results were supported by nematode killing assays and experiments using wax moth larvae as invertebrate model systems.ConclusionsOur data indicate that the coil-coiled domain of DIP0733 is crucial for interaction with epithelial cells and pathogenicity in invertebrate animal model systems.Electronic supplementary materialThe online version of this article (10.1186/s12866-018-1247-z) contains supplementary material, which is available to authorized users.

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Fibrinogen binds to nontoxigenic and toxigenic Corynebacterium diphtheriae strains

Cited by 20 publications

References 38 publications

Biofilm production by multiresistant Corynebacterium striatumassociated with nosocomial outbreak

Biofilm production by multiresistant Corynebacterium striatumassociated with nosocomial outbreak

Characterization of DIP0733, a multi-functional virulence factor of Corynebacterium diphtheriae

The C-terminal coiled-coil domain of Corynebacterium diphtheriae DIP0733 is crucial for interaction with epithelial cells and pathogenicity in invertebrate animal model systems

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