PavA of<i>Streptococcus pneumoniae</i>Modulates Adherence, Invasion, and Meningeal Inflammation

Pracht, Daniela; Elm, Christine; Gerber, Joachim; Bergmann, Simone; Rohde, Manfred; Seiler, Marleen; Kim, Kwang S.; Jenkinson, Howard F.; Nau, Roland; Hammerschmidt, Sven

doi:10.1128/iai.73.5.2680-2689.2005

Cited by 158 publications

(207 citation statements)

References 60 publications

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“…The PavA protein (pneumococcal adherence and virulence factor A) has been identified as a pneumococcal adhesin for fibronectin and as a crucial virulence determinant in pneumococcal infections. In a systemic and experimental mouse meningitis model of infection, the pneumococcal pavA knockout of strain D39 is substantially attenuated (Holmes et al, 2001;Pracht et al, 2005). The impact of PavA on pathogenesis has been independently indicated by STM experiments using a mouse pneumonia model of infection (Lau et al, 2001).…”

Section: Moonlighting Proteins: Keeping the Secretmentioning

confidence: 99%

“…In addition, PavA is most likely involved indirectly and in a fibronectin-independent manner in pneumococcal adherence to host cells. However, the precise function of PavA has yet to be clarified, because deficiency in PavA does not affect the expression and function of known virulence factors (Pracht et al, 2005).…”

Section: Moonlighting Proteins: Keeping the Secretmentioning

confidence: 99%

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Versatility of pneumococcal surface proteins

2006

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Surface-exposed proteins are key players during the infectious process of pathogenic bacteria. The cell surface of the Gram-positive human pathogen Streptococcus pneumoniae is decorated not only by typical Gram-positive surface proteins, but also by a family of proteins that recognizes the phosphorylcholine of the lipoteichoic and teichoic acids, namely the choline-binding proteins, and by non-classical surface proteins that lack a leader peptide and membrane-anchor motif. A comprehensive understanding of how microbial proteins subvert host immunity or host protein functions is a prerequisite for the development of novel therapeutic strategies to combat pneumococcal infections. This article reviews recent progress in the investigation of the versatility and sophistication of the virulence functions of surface-exposed pneumococcal proteins.

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Section: Moonlighting Proteins: Keeping the Secretmentioning

confidence: 99%

Section: Moonlighting Proteins: Keeping the Secretmentioning

confidence: 99%

Versatility of pneumococcal surface proteins

2006

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“…Pneumococci are equipped with three different types of fibronectin-binding proteins: pneumococcal adherence and virulence factor A (PavA); plasmin-fibronectin binding protein A (PfbA); and pneumococcal endopeptidase O (PepO), which mediate adhesion to airway epithelia [10,35,36]. Adherence of NTHi to fibronectin, laminin and type IV collagen is mediated by an autotransporter, Haemophilus adhesion and penetration protein (Hap) [37].…”

Section: Temporal Host Surface Receptor Upregulation In Different Bodmentioning

confidence: 99%

“…ligament rupture) as a natural response to tissue repair. It is, therefore, an attractive target for adherence and invasion by several bacterial pathogens, such as Neisseria meningitidis, Streptococcus pneumoniae and non-typeable Haemophilus influenzae (NTHi) [3,[7][8][9][10][11].…”

Section: Host Surface Receptors For Bacterial Colonizationmentioning

confidence: 99%

Temporal upregulation of host surface receptors provides a window of opportunity for bacterial adhesion and disease

Shukla

Walters

et al. 2017

Microbiology

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Host surface receptors provide bacteria with a foothold from which to attach, colonize and, in some cases, invade tissue and elicit human disease. In this review, we discuss several key host receptors and cognate adhesins that function in bacterial pathogenesis. In particular, we examine the elevated expression of host surface receptors such as CEACAM-1, CEACAM-6, ICAM-1 and PAFR in response to specific stimuli. We explore how upregulated receptors, in turn, expose the host to a range of bacterial infections in the respiratory tract. It is apparent that exploitation of receptor induction for bacterial adherence is not unique to one body system, but is also observed in the central nervous, gastrointestinal and urogenital systems. Prokaryotic pathogens which utilize this mechanism for their infectivity include Streptococcus pneumoniae, Haemophilus influenzae, Neisseria meningitidis and Escherichia coli. A number of approaches have been used, in both in vitro and in vivo experimental models, to inhibit bacterial attachment to temporally expressed host receptors. Some of these novel strategies may advance future targeted interventions for the prevention and treatment of bacterial disease.

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“…Although PavA is homologous to Fn-binding proteins of other pathogens (e.g. Fbp54 of Streptococcus pyogenes or FbpA of Listeria monocytogenes), it is likely that PavA does not bind directly to Fn but rather modulates the surface expression of other adhesins that are directly responsible for this interaction (15). Recently, a protein designated as PfbA (standing for plasmin-and fibronectin-binding protein A) was reported to bind to Fn, plasminogen, plasmin, and human serum albumin (16).…”

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confidence: 99%

Plasminogen- and Fibronectin-binding Protein B Is Involved in the Adherence of Streptococcus pneumoniae to Human Epithelial Cells

Papasergi

Garibaldi

Tuscano

et al. 2010

Journal of Biological Chemistry

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Streptococcus pneumoniae is a major cause of morbidity and mortality worldwide. The ability of this bacterium to adhere to epithelial cells is considered as an essential early step in colonization and infection. By screening a whole genome phage display library with sera from infected patients, we previously identified three antigenic fragments matching open reading frame spr0075 of the strain R6 genome. This locus encodes for an ϳ120-kDa protein, herein referred to as plasminogen-and fibronectin-binding protein B (PfbB), which displays an LPXTG cell wall anchoring motif and six repetitive domains. In this study, by using isogenic pfbB-deleted mutants of the encapsulated D39 and of the unencapsulated DP1004 type 2 pneumococcal strains, we show that PfbB is involved in S. pneumoniae adherence to various epithelial respiratory tract cell lines. Our data suggest that PfbB directly mediates bacterial adhesion, because fluorescent beads coated with the recombinant PfbB sp17 fragment (encompassing one of the six repetitive domains and the C-terminal region) efficiently bound to epithelial cells. Mutants lacking PfbB bound to fibronectin and plasminogen considerably less efficiently than wild type bacteria, whereas sp17-coated beads specifically bound to both of these substrates. Taken together, our data suggest that, by directly interacting with fibronectin, PfbB significantly increases the ability of S. pneumoniae to adhere to human epithelial cells.

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PavA ofStreptococcus pneumoniaeModulates Adherence, Invasion, and Meningeal Inflammation

Cited by 158 publications

References 60 publications

Versatility of pneumococcal surface proteins

Versatility of pneumococcal surface proteins

Temporal upregulation of host surface receptors provides a window of opportunity for bacterial adhesion and disease

Plasminogen- and Fibronectin-binding Protein B Is Involved in the Adherence of Streptococcus pneumoniae to Human Epithelial Cells

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