TY - JOUR
T1 - Flamingo cadherin
T2 - A putative host receptor for Streptococcus pneumoniae
AU - Blau, Karin
AU - Portnoi, Maxim
AU - Shagan, Marilou
AU - Kaganovich, Antonina
AU - Rom, Slava
AU - Kafka, Daniel
AU - Caspi, Vered Chalifa
AU - Porgador, Angel
AU - Givon-Lavi, Noga
AU - Gershoni, Jonathan M.
AU - Dagan, Ron
AU - Nebenzahl, Yaffa Mizrachi
PY - 2007/6/15
Y1 - 2007/6/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=34249908935&partnerID=8YFLogxK
U2 - 10.1086/518038
DO - 10.1086/518038
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C2 - 17492599
AN - SCOPUS:34249908935
SN - 0022-1899
VL - 195
SP - 1828
EP - 1837
JO - Journal of Infectious Diseases
JF - Journal of Infectious Diseases
IS - 12
ER -