Overexpression, purification and crystallization of a choline-binding protein CbpI from<i>Streptococcus pneumoniae</i>

Paterson, Neil G.; Riboldi-Tunicliffe, Alan; Mitchell, Tim; Isaacs, Neil W.

doi:10.1107/s1744309106020616

Cited by 4 publications

(3 citation statements)

References 15 publications

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“…However, cbpI was the only CBP gene that was identified in this study. The function of CbpI is still unclear but its crystal structure has been solved [ 17 ]. Whether it is important in colonization, most CBPs might not be required at the early stage of interaction with host epithelial cells.…”

Section: Resultsmentioning

confidence: 99%

Streptococcus pneumoniae early response genes to human lung epithelial cells

et al. 2008

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Background: Streptococcus pneumoniae infection starts from colonization of the host respiratory tract where interaction with host respiratory tract epithelial cells occurs. To investigate pneumococcal genes that are involved in the early stage of interaction with host epithelial cells, transcriptional responses of an encapsulated pathogenic pneumococcal strain TIGR4 upon exposure to human lung epithelial cells A549 for 0.5 h and 1 h time periods were investigated by using TIGR (JCVI) microarray technology. Gene expression changes were validated by quantitative real-time PCR (qRT-PCR) analysis.

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Section: Resultsmentioning

confidence: 99%

Streptococcus pneumoniae early response genes to human lung epithelial cells

et al. 2008

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“…Besides sequence information, little is known about CbpI and CbpJ. Preliminary crystallization data of CbpI (Paterson et al , 2006) are available.…”

Section: Other Pneumococcal Cbpsmentioning

confidence: 99%

Versatility of choline metabolism and choline-binding proteins inStreptococcus pneumoniaeand commensal streptococci

et al. 2009

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The pneumococcal choline-containing teichoic acids are targeted by cholinebinding proteins (CBPs), major surface components implicated in the interaction with host cells and bacterial cell physiology. CBPs also occur in closely related commensal species, Streptococcus oralis and Streptococcus mitis, and many strains of these species contain choline in their cell wall. Physiologically relevant CBPs including cell wall lytic enzymes are highly conserved between Streptococcus pneumoniae and S. mitis. In contrast, the virulence-associated CBPs, CbpA, PspA and PcpA, are S. pneumoniae specific and are thus relevant for the characteristic properties of this species.

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“…The bp I gene SP0069 in S. pneumoniae is present in TIGR4, but not in other studied strains such as R6, Hu19A_6, CGSP14 or the multiresistant Sanger 23F −1 [ 43 ]. It codes for a protein, CbpI, which has been crystallized, although the structure has not been elucidated yet [ 190 ]. It presents an N-terminal sequence without homology with other previously identified CBPs, and a CBM in the C-terminus with 5 CBRs [ 58 ].…”

Section: Pneumococcal Host-encoded Cbpsmentioning

confidence: 99%

Choline Binding Proteins from Streptococcus pneumoniae: A Dual Role as Enzybiotics and Targets for the Design of New Antimicrobials

2016

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Streptococcus pneumoniae (pneumococcus) is an important pathogen responsible for acute invasive and non-invasive infections such as meningitis, sepsis and otitis media, being the major cause of community-acquired pneumonia. The fight against pneumococcus is currently hampered both by insufficient vaccine coverage and by rising antimicrobial resistances to traditional antibiotics, making necessary the research on novel targets. Choline binding proteins (CBPs) are a family of polypeptides found in pneumococcus and related species, as well as in some of their associated bacteriophages. They are characterized by a structural organization in two modules: a functional module (FM), and a choline-binding module (CBM) that anchors the protein to the choline residues present in the cell wall through non-covalent interactions. Pneumococcal CBPs include cell wall hydrolases, adhesins and other virulence factors, all playing relevant physiological roles for bacterial viability and virulence. Moreover, many pneumococcal phages also make use of hydrolytic CBPs to fulfill their infectivity cycle. Consequently, CBPs may play a dual role for the development of novel antipneumococcal drugs, both as targets for inhibitors of their binding to the cell wall and as active cell lytic agents (enzybiotics). In this article, we review the current state of knowledge about host- and phage-encoded pneumococcal CBPs, with a special focus on structural issues, together with their perspectives for effective anti-infectious treatments.

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Overexpression, purification and crystallization of a choline-binding protein CbpI fromStreptococcus pneumoniae

Cited by 4 publications

References 15 publications

Streptococcus pneumoniae early response genes to human lung epithelial cells

Streptococcus pneumoniae early response genes to human lung epithelial cells

Versatility of choline metabolism and choline-binding proteins inStreptococcus pneumoniaeand commensal streptococci

Choline Binding Proteins from Streptococcus pneumoniae: A Dual Role as Enzybiotics and Targets for the Design of New Antimicrobials

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