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
Rok vydání: 2007
Předmět:
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