scholarly journals In Silico design of an epitope-based vaccine against Choline binding protein A of Streptococcus pneumoniae

2021 ◽  
pp. 100546
Author(s):  
Meherunnesa Munia ◽  
Shafi Mahmud ◽  
Mohammed Mohasin ◽  
K.M.Kaderi Kibria
Keyword(s):  
Streptococcus Pneumoniae ◽  
In Silico ◽  
Binding Protein ◽  
Protein A ◽  
In Silico Design

scholarly journals A bivalent pneumococcal histidine triad protein D-choline-binding protein A vaccine elicits functional antibodies that passively protect mice from Streptococcus pneumoniae challenge

2016 ◽  
Vol 12 (11) ◽  
pp. 2946-2952 ◽  
Author(s):  
Martina M. Ochs ◽  
Kimberley Williams ◽  
Anthony Sheung ◽  
Philippe Lheritier ◽  
Lucian Visan ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Binding Protein ◽  
Protein A ◽  
Functional Antibodies

scholarly journals The Human Polymeric Immunoglobulin Receptor Facilitates Invasion of Epithelial Cells by Streptococcus pneumoniae in a Strain-Specific and Cell Type-Specific Manner

2002 ◽  
Vol 70 (9) ◽  
pp. 5091-5095 ◽  
Author(s):  
Sean C. Brock ◽  
Patricia A. McGraw ◽  
Peter F. Wright ◽  
James E. Crowe
Keyword(s):  
Streptococcus Pneumoniae ◽  
Epithelial Cells ◽  
Binding Protein ◽  
Protein A ◽  
Respiratory Epithelium ◽  
Polymeric Immunoglobulin Receptor ◽  
Cell Type ◽  
Immunoglobulin Receptor ◽  
Specific Manner ◽  
Cell Type Specific

ABSTRACT Streptococcus pneumoniae is a gram-positive bacterial pathogen that causes invasive life-threatening disease worldwide. This organism also commonly colonizes the upper respiratory epithelium in an asymptomatic fashion. To invade, this pathogen must traverse the respiratory epithelial barrier, allowing it to cause disease locally or disseminate hematogenously throughout the body. Previous work has demonstrated that S. pneumoniae choline-binding protein A, a pneumococcal surface protein, interacts specifically with the human polymeric immunoglobulin receptor, which is expressed by cells in the respiratory epithelium. Choline-binding protein A is required for efficient colonization of the nasopharynx in vivo. Additionally, a recent study showed that the R6x laboratory strain of S. pneumoniae invades a human pharyngeal cell line in a human polymeric immunoglobulin receptor-dependent manner. These findings raised the possibility that the interaction between choline-binding protein A and human polymeric immunoglobulin receptor may be a key determinant of S. pneumoniae pathogenesis. However, the strain used in prior invasion studies, R6x, is an unencapsulated, nonpathogenic strain. In the present study we determined the relative ability of strain R6x or pathogenic strains to invade a variety of human polymeric immunoglobulin receptor-expressing epithelial cell lines. The results of this work suggest that human polymeric immunoglobulin receptor-dependent enhanced invasion of epithelial cells by S. pneumoniae is a limited phenomenon that occurs in a strain-specific and cell type-specific manner.

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 Solution structure of choline binding protein A, the major adhesin of Streptococcus pneumoniae

2004 ◽  
Vol 24 (1) ◽  
pp. 34-43 ◽  
Author(s):  
Rensheng Luo ◽  
Beth Mann ◽  
William S Lewis ◽  
Arthur Rowe ◽  
Richard Heath ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Solution Structure ◽  
Binding Protein ◽  
Protein A

scholarly journals Structural determinants of host specificity of complement Factor H recruitment by Streptococcus pneumoniae

2015 ◽  
Vol 465 (2) ◽  
pp. 325-335 ◽  
Author(s):  
David Achila ◽  
Aizhuo Liu ◽  
Rahul Banerjee ◽  
Yue Li ◽  
Erik Martinez-Hackert ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Host Specificity ◽  
Atomic Structure ◽  
Binding Protein ◽  
Protein A ◽  
Factor H ◽  
Complement Factor H ◽  
Complement Factor ◽  
Human Complement ◽  
Structural Determinants

The complex of human complement Factor H (FH) and pneumococcal protein CbpA (choline-binding protein A) enables S. pneumoniae to evade phagocytosis and contributes to pneumococcal host specificity. The present work elucidates the atomic structure of the complex and the structural determinants of its host specificity.

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