Flamingo Cadherin: A Putative Host Receptor forStreptococcus pneumoniae
| العنوان: | Flamingo Cadherin: A Putative Host Receptor forStreptococcus pneumoniae |
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| المؤلفون: | 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 |
| المصدر: | The Journal of Infectious Diseases. 195:1828-1837 |
| بيانات النشر: | Oxford University Press (OUP), 2007. |
| سنة النشر: | 2007 |
| مصطلحات موضوعية: | 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 |
| الوصف: | 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. |
| تدمد: | 1537-6613 0022-1899 |
| DOI: | 10.1086/518038 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::871f4fcbf8d2bf2287ebfa03bbcfc5a9 https://doi.org/10.1086/518038 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....871f4fcbf8d2bf2287ebfa03bbcfc5a9 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15376613 00221899 |
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| DOI: | 10.1086/518038 |