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New adhesin functions of surface-exposed pneumococcal proteins
BACKGROUND: Streptococcus pneumoniae is a widely distributed commensal Gram-positive bacteria of the upper respiratory tract. Pneumococcal colonization can progress to invasive disease, and thus become lethal, reason why antibiotics and vaccines are designed to limit the dramatic effects of the bact...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2911433/ https://www.ncbi.nlm.nih.gov/pubmed/20624274 http://dx.doi.org/10.1186/1471-2180-10-190 |
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author | Frolet, Cécile Beniazza, Meryam Roux, Laure Gallet, Benoit Noirclerc-Savoye, Marjolaine Vernet, Thierry Di Guilmi, Anne Marie |
author_facet | Frolet, Cécile Beniazza, Meryam Roux, Laure Gallet, Benoit Noirclerc-Savoye, Marjolaine Vernet, Thierry Di Guilmi, Anne Marie |
author_sort | Frolet, Cécile |
collection | PubMed |
description | BACKGROUND: Streptococcus pneumoniae is a widely distributed commensal Gram-positive bacteria of the upper respiratory tract. Pneumococcal colonization can progress to invasive disease, and thus become lethal, reason why antibiotics and vaccines are designed to limit the dramatic effects of the bacteria in such cases. As a consequence, pneumococcus has developed efficient antibiotic resistance, and the use of vaccines covering a limited number of serotypes such as Pneumovax(® )and Prevnar(® )results in the expansion of non-covered serotypes. Pneumococcal surface proteins represent challenging candidates for the development of new therapeutic targets against the bacteria. Despite the number of described virulence factors, we believe that the majority of them remain to be characterized. This is the reason why pneumococcus invasion processes are still largely unknown. RESULTS: Availability of genome sequences facilitated the identification of pneumococcal surface proteins bearing characteristic motifs such as choline-binding proteins (Cbp) and peptidoglycan binding (LPXTG) proteins. We designed a medium throughput approach to systematically test for interactions between these pneumococcal surface proteins and host proteins (extracellular matrix proteins, circulating proteins or immunity related proteins). We cloned, expressed and purified 28 pneumococcal surface proteins. Interactions were tested in a solid phase assay, which led to the identification of 23 protein-protein interactions among which 20 are new. CONCLUSIONS: We conclude that whether peptidoglycan binding proteins do not appear to be major adhesins, most of the choline-binding proteins interact with host proteins (elastin and C reactive proteins are the major Cbp partners). These newly identified interactions open the way to a better understanding of host-pneumococcal interactions. |
format | Text |
id | pubmed-2911433 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-29114332010-07-29 New adhesin functions of surface-exposed pneumococcal proteins Frolet, Cécile Beniazza, Meryam Roux, Laure Gallet, Benoit Noirclerc-Savoye, Marjolaine Vernet, Thierry Di Guilmi, Anne Marie BMC Microbiol Research Article BACKGROUND: Streptococcus pneumoniae is a widely distributed commensal Gram-positive bacteria of the upper respiratory tract. Pneumococcal colonization can progress to invasive disease, and thus become lethal, reason why antibiotics and vaccines are designed to limit the dramatic effects of the bacteria in such cases. As a consequence, pneumococcus has developed efficient antibiotic resistance, and the use of vaccines covering a limited number of serotypes such as Pneumovax(® )and Prevnar(® )results in the expansion of non-covered serotypes. Pneumococcal surface proteins represent challenging candidates for the development of new therapeutic targets against the bacteria. Despite the number of described virulence factors, we believe that the majority of them remain to be characterized. This is the reason why pneumococcus invasion processes are still largely unknown. RESULTS: Availability of genome sequences facilitated the identification of pneumococcal surface proteins bearing characteristic motifs such as choline-binding proteins (Cbp) and peptidoglycan binding (LPXTG) proteins. We designed a medium throughput approach to systematically test for interactions between these pneumococcal surface proteins and host proteins (extracellular matrix proteins, circulating proteins or immunity related proteins). We cloned, expressed and purified 28 pneumococcal surface proteins. Interactions were tested in a solid phase assay, which led to the identification of 23 protein-protein interactions among which 20 are new. CONCLUSIONS: We conclude that whether peptidoglycan binding proteins do not appear to be major adhesins, most of the choline-binding proteins interact with host proteins (elastin and C reactive proteins are the major Cbp partners). These newly identified interactions open the way to a better understanding of host-pneumococcal interactions. BioMed Central 2010-07-12 /pmc/articles/PMC2911433/ /pubmed/20624274 http://dx.doi.org/10.1186/1471-2180-10-190 Text en Copyright ©2010 Frolet et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Frolet, Cécile Beniazza, Meryam Roux, Laure Gallet, Benoit Noirclerc-Savoye, Marjolaine Vernet, Thierry Di Guilmi, Anne Marie New adhesin functions of surface-exposed pneumococcal proteins |
title | New adhesin functions of surface-exposed pneumococcal proteins |
title_full | New adhesin functions of surface-exposed pneumococcal proteins |
title_fullStr | New adhesin functions of surface-exposed pneumococcal proteins |
title_full_unstemmed | New adhesin functions of surface-exposed pneumococcal proteins |
title_short | New adhesin functions of surface-exposed pneumococcal proteins |
title_sort | new adhesin functions of surface-exposed pneumococcal proteins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2911433/ https://www.ncbi.nlm.nih.gov/pubmed/20624274 http://dx.doi.org/10.1186/1471-2180-10-190 |
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