Inhibition of anion transport in human erythrocytes by pilated Neisseria gonorrhoeae.
Pilated gonococci added to human erythrocytes apparently bind to polypeptide band 3 and inhibit chloride-bicarbonate exchange across the membrane in contrast with nonpilated organisms. Known covalent inhibitors of anion transport (4,4'-diisothiocyano-2,2'-disulphonic acid stilbene and alpha-cyano-4-hydroxycinnamic acid) inhibit chloride efflux from erythrocytes and also reduce hemagglutination titres, strongly suggesting that band 3 is the major host-cell receptor involved in all interaction between gonococci and erythrocytes. In studies of other cell species, however, band 3 prepared from human erythrocytes inhibited adherence of pilated gonococci to human foreskin and HeLa cells, but was without effect in human buccal, Vero, and mouse L cells.
D000268:Adhesiveness; D001692:Biological Transport; D001798:Blood Proteins / Q000378:metabolism; D002712:Chlorides / Q000097:blood*; D004912:Erythrocytes / Q000378:metabolism*; D010861:Fimbriae, Bacterial / Q000502:physiology; D006384:Hemagglutination; D006801:Humans; D066298:In Vitro Techniques; D009344:Neisseria gonorrhoeae / Q000472:pathogenicity / Q000502:physiology*
D001798:Blood Proteins; D002712:Chlorides