Cell-free solution of choline-binding protein of Streptococcus pneumoniae; especially pneumococcal surface protein-A prepared by treating cells with choline and useful as an immunogen in vaccine composition

Vaccine ◽  
1994 ◽  
Vol 12 (8) ◽  
pp. 767
Keyword(s):  
Streptococcus Pneumoniae ◽  
Binding Protein ◽  
Protein A ◽  
Surface Protein ◽  
Free Solution ◽  
Pneumococcal Surface Protein A

scholarly journals Identification of Pneumococcal Surface Protein A as a Lactoferrin-Binding Protein of Streptococcus pneumoniae

1999 ◽  
Vol 67 (4) ◽  
pp. 1683-1687 ◽  
Author(s):  
Sven Hammerschmidt ◽  
Gesina Bethe ◽  
Petra H. Remane ◽  
Gursharan S. Chhatwal
Keyword(s):  
Streptococcus Pneumoniae ◽  
Binding Protein ◽  
Protein A ◽  
Surface Protein ◽  
Pneumococcal Surface Protein A

scholarly journals Identification of Pneumococcal Surface Protein A as a Lactoferrin-Binding Protein of Streptococcus pneumoniae

1999 ◽  
Vol 67 (4) ◽  
pp. 1683-1687 ◽  
Author(s):  
Sven Hammerschmidt ◽  
Gesina Bethe ◽  
Petra H. Remane ◽  
Gursharan S. Chhatwal
Keyword(s):  
Streptococcus Pneumoniae ◽  
Bacterial Infections ◽  
Dissociation Constants ◽  
Binding Protein ◽  
Protein A ◽  
Surface Protein ◽  
Scatchard Analysis ◽  
Binding Assays ◽  
Pneumococcal Surface Protein A ◽  
Mucosal Surfaces

ABSTRACT Lactoferrin (Lf), an iron-sequestering glycoprotein, predominates in mucosal secretions, where the level of free extracellular iron (10−18 M) is not sufficient for bacterial growth. This represents a mechanism of resistance to bacterial infections by prevention of colonization of the host by pathogens. In this study we were able to show that Streptococcus pneumoniaespecifically recognizes and binds the iron carrier protein human Lf (hLf). Pretreatment of pneumococci with proteases reduced hLf binding significantly, indicating that the hLf receptor is proteinaceous. Binding assays performed with 63 clinical isolates belonging to different serotypes showed that 88% of the tested isolates interacted with hLf. Scatchard analysis showed the existence of two hLf-binding proteins with dissociation constants of 5.7 × 10−8and 2.74 × 10−7 M. The receptors were purified by affinity chromatography, and internal sequence analysis revealed that one of the S. pneumoniae proteins was homologous to pneumococcal surface protein A (PspA). The function of PspA as an hLf-binding protein was confirmed by the ability of purified PspA to bind hLf and to competitively inhibit hLf binding to pneumococci.S. pneumoniae may use the hLf-PspA interaction to overcome the iron limitation at mucosal surfaces, and this might represent a potential virulence mechanism.

scholarly journals DNA vaccines expressing pneumococcal surface protein A (PspA) elicit protection levels comparable to recombinant protein

2006 ◽  
Vol 55 (4) ◽  
pp. 375-378 ◽  
Author(s):  
Daniela M. Ferreira ◽  
Eliane N. Miyaji ◽  
Maria Leonor S. Oliveira ◽  
Michelle Darrieux ◽  
Ana Paula M. Arêas ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Recombinant Protein ◽  
Dna Vaccines ◽  
Protein A ◽  
Surface Protein ◽  
Humoral Response ◽  
Cost Effective ◽  
Promising Candidate ◽  
Pneumococcal Surface Protein A ◽  
Antibody Levels

Pneumococcal surface protein A (PspA) is a promising candidate for the development of cost-effective vaccines against Streptococcus pneumoniae. In the present study, BALB/c mice were immunized with DNA vaccine vectors expressing the N-terminal region of PspA. Animals immunized with a vector expressing secreted PspA developed higher levels of antibody than mice immunized with the vector expressing the antigen in the cytosol. However, both immunogens elicited similar levels of protection against intraperitoneal challenge. Furthermore, immunization with exactly the same fragment in the form of a recombinant protein, with aluminium hydroxide as an adjuvant, elicited even higher antibody levels, but this increased humoral response did not correlate with enhanced protection. These results show that DNA vaccines expressing PspA are able to elicit protection levels comparable to recombinant protein, even though total anti-PspA IgG response is considerably lower.

scholarly journals Characterization of the antibody response elicited by immunization with pneumococcal surface protein A (PspA) as recombinant protein or DNA vaccine and analysis of protection against an intranasal lethal challenge with Streptococcus pneumoniae

2012 ◽  
Vol 53 (5-6) ◽  
pp. 243-249 ◽  
Author(s):  
Cintia F.M. Vadesilho ◽  
Daniela M. Ferreira ◽  
Adriana T. Moreno ◽  
Carlos Chavez-Olortegui ◽  
Ricardo A. Machado de Avila ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Recombinant Protein ◽  
Antibody Response ◽  
Dna Vaccine ◽  
Protein A ◽  
Surface Protein ◽  
Lethal Challenge ◽  
Pneumococcal Surface Protein A

scholarly journals Correction: Generation and Improvement of Effector Function of a Novel Broadly Reactive and Protective Monoclonal Antibody against Pneumococcal Surface Protein A of Streptococcus pneumoniae

PLoS ONE ◽  
2017 ◽  
Vol 12 (2) ◽  
pp. e0171732
Author(s):  
Sascha A. Kristian ◽  
Takayuki Ota ◽  
Sarah S. Bubeck ◽  
Rebecca Cho ◽  
Brian C. Groff ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Streptococcus Pneumoniae ◽  
Protein A ◽  
Surface Protein ◽  
Effector Function ◽  
Pneumococcal Surface Protein A ◽  
Correction Generation

scholarly journals Determination of phenotypes and pneumococcal surface protein A family types of Streptococcus pneumoniae from Malaysian healthy children

2013 ◽  
Vol 46 (3) ◽  
pp. 180-186 ◽  
Author(s):  
Masura Mohd Yatim ◽  
Siti Norbaya Masri ◽  
Mohd Nasir Mohd Desa ◽  
Niazlin Mohd Taib ◽  
Syafinaz Amin Nordin ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Protein A ◽  
Surface Protein ◽  
Healthy Children ◽  
Pneumococcal Surface Protein A ◽  
Family Types

Genetic diversity of pneumococcal surface protein A of Streptococcus pneumoniae meningitis in German children

Vaccine ◽  
2007 ◽  
Vol 25 (6) ◽  
pp. 1030-1035 ◽  
Author(s):  
Christiane Heeg ◽  
Carmen Franken ◽  
Mark van der Linden ◽  
Adnan Al-Lahham ◽  
Ralf René Reinert
Keyword(s):  
Genetic Diversity ◽  
Streptococcus Pneumoniae ◽  
Protein A ◽  
Surface Protein ◽  
Pneumococcal Surface Protein A ◽  
German Children

scholarly journals Contributions of Pneumolysin, Pneumococcal Surface Protein A (PspA), and PspC to Pathogenicity of Streptococcus pneumoniae D39 in a Mouse Model

2007 ◽  
Vol 75 (4) ◽  
pp. 1843-1851 ◽  
Author(s):  
Abiodun D. Ogunniyi ◽  
Kim S. LeMessurier ◽  
Rikki M. A. Graham ◽  
James M. Watt ◽  
David E. Briles ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Systemic Disease ◽  
Protein A ◽  
Virulence Gene ◽  
Surface Protein ◽  
Invasive Disease ◽  
Upper Respiratory Tract ◽  
Virulence Proteins ◽  
Pneumococcal Surface Protein A ◽  
Genes Encoding

ABSTRACTSuccessful colonization of the upper respiratory tract byStreptococcus pneumoniaeis an essential first step in the pathogenesis of pneumococcal disease. However, the bacterial and host factors that provoke the progression from asymptomatic colonization to invasive disease are yet to be fully defined. In this study, we investigated the effects of single and combined mutations in genes encoding pneumolysin (Ply), pneumococcal surface protein A (PspA), and pneumococcal surface protein C (PspC, also known as choline-binding protein A) on the pathogenicity ofStreptococcus pneumoniaeserotype 2 (D39) in mice. Following intranasal challenge with D39, stable colonization of the nasopharynx was maintained over a 7-day period at a level of approximately 105bacteria per mouse. The abilities of the mutant deficient in PspA to colonize the nasopharynx and to cause lung infection and bacteremia were significantly reduced. Likewise, the PspC mutant and, to a lesser extent, the Ply mutant also had reduced abilities to colonize the nasopharynx. As expected, the double mutants colonized less well than the parent to various degrees and had difficulty translocating to the lungs and blood. A significant additive attenuation was observed for the double and triple mutants in pneumonia and systemic disease models. Surprisingly, the colonization profile of the derivative lacking all three proteins was similar to that of the wild type, indicating virulence gene compensation. These findings further demonstrate that the mechanism of pneumococcal pathogenesis is highly complex and multifactorial but ascribes a role for each of these virulence proteins, alone or in combination, in the process.

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