Flamingo Cadherin: A Putative Host Receptor forStreptococcus pneumoniae
Autor: | Karin Blau, Noga Givon-Lavi, Angel Porgador, Vered Chalifa Caspi, Marilou Shagan, Slava Rom, Jonathan M. Gershoni, Ron Dagan, Yaffa Mizrachi Nebenzahl, Maxim Portnoi, Daniel Kafka, Antonina Kaganovich |
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Rok vydání: | 2007 |
Předmět: |
Time Factors
Virus Attachment Fructose-bisphosphate aldolase Biology medicine.disease_cause Bacterial Adhesion Pneumococcal Infections law.invention Microbiology Mice law Cell Line Tumor Fructose-Bisphosphate Aldolase Nasopharynx Streptococcus pneumoniae medicine Animals Humans Immunology and Allergy Adhesins Bacterial Peptide library Peptide sequence Mice Inbred BALB C Sequence Homology Amino Acid Cadherin Cadherins Antibodies Bacterial Recombinant Proteins respiratory tract diseases Bacterial adhesin Infectious Diseases Recombinant DNA biology.protein Female Rabbits Antibody |
Zdroj: | The Journal of Infectious Diseases. 195:1828-1837 |
ISSN: | 1537-6613 0022-1899 |
DOI: | 10.1086/518038 |
Popis: | Streptococcus pneumoniae fructose bisphosphate aldolase (FBA) is a cell wall-localized lectin. We demonstrate that recombinant (r) FBA and anti-rFBA antibodies inhibit encapsulated and unencapsulated S. pneumoniae serotype 3 adherence to A549 type II lung carcinoma epithelial cells. A random combinatorial peptide library expressed by filamentous phage was screened with rFBA. Eleven of 30 rFBA-binding phages inhibited 90% of S. pneumoniae adhesion to A549 cells. The insert peptide sequence of 9 of these phages matched the Flamingo cadherin receptor (FCR) when aligned against the human genome. A peptide comprising a putative FBA-binding region of FCR (FCRP) inhibited 2 genetically and capsularly unrelated pairs of encapsulated and unencapsulated S. pneumoniae strains from binding to A549 cells. Moreover, FCRP inhibited S. pneumoniae nasopharyngeal and lung colonization and, possibly, pneumonia development in the mouse intranasal inoculation model system. These data indicate that FBA is an S. pneumoniae adhesin and that FCR is its host receptor. |
Databáze: | OpenAIRE |
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