Flamingo cadherin: A putative host receptor for Streptococcus pneumoniae

Karin Blau, Maxim Portnoi, Marilou Shagan, Antonina Kaganovich, Slava Rom, Daniel Kafka, Vered Chalifa Caspi, Angel Porgador, Noga Givon-Lavi, Jonathan M. Gershoni, Ron Dagan, Yaffa Mizrachi Nebenzahl*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)1828-1837
Number of pages10
JournalJournal of Infectious Diseases
Issue number12
StatePublished - 15 Jun 2007


Dive into the research topics of 'Flamingo cadherin: A putative host receptor for Streptococcus pneumoniae'. Together they form a unique fingerprint.

Cite this