The polymeric immunoglobulin receptor translocates pneumococci across human nasopharyngeal epithelial cells.
The polymeric immunoglobulin receptor (pIgR) plays a crucial role in mucosal immunity against microbial infection by transporting polymeric immunoglobulins (pIg) across the mucosal epithelium. We report here that the human pIgR (hpIgR) can bind to a major pneumococcal adhesin, CbpA. Expression of hpIgR in human nasopharyngeal cells and MDCK cells greatly enhanced pneumococcal adherence and invasion. The hpIgR-mediated bacterial adherence and invasion were abolished by either insertional knockout of cbpA or antibodies against either hpIgR or CbpA. In contrast, rabbit pIgR (rpIgR) did not bind to CbpA and its expression in MDCK cells did not enhance pneumococcal adherence and invasion. These results suggest that pneumococci are a novel example of a pathogen co-opting the pIg transcytosis machinery to promote translocation across a mucosal barrier.
Zhang
J R
JR
Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
Mostov
K E
KE
Lamm
M E
ME
Nanno
M
M
Shimida
S
S
Ohwaki
M
M
Tuomanen
E
E
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D001422:Bacterial Adhesion / Q000502:physiology; D001426:Bacterial Proteins; D002460:Cell Line; D004268:DNA-Binding Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D004847:Epithelial Cells / Q000378:metabolism / Q000382:microbiology*; D006360:Heat-Shock Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D006801:Humans; D007668:Kidney / Q000166:cytology; D008099:Liver / Q000166:cytology; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D008863:Microspheres; D008969:Molecular Sequence Data; D009297:Nasal Mucosa / Q000166:cytology / Q000276:immunology / Q000382:microbiology*; D010614:Pharynx / Q000166:cytology / Q000276:immunology / Q000382:microbiology; D010980:Platelet Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism; D011008:Pneumococcal Infections / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary; D011817:Rabbits; D011956:Receptors, Cell Surface; D043562:Receptors, G-Protein-Coupled; D019056:Receptors, Polymeric Immunoglobulin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013296:Streptococcus pneumoniae / Q000378:metabolism*
D000906:Antibodies; D001426:Bacterial Proteins; C490083:CbpA protein, bacteria; D004268:DNA-Binding Proteins; D006360:Heat-Shock Proteins; D010980:Platelet Membrane Glycoproteins; D011956:Receptors, Cell Surface; D043562:Receptors, G-Protein-Coupled; D019056:Receptors, Polymeric Immunoglobulin; C039351:platelet activating factor receptor