Influence of adhesins on the interaction of Escherichia coli with human phagocytes

Abstract

The fitness between bacterial adhesins and target cell receptors, determining bacterial adherence to epithelial cells in urinary tract infections, was shown to influence also the interaction with human polymorphonuclear leukocytes (PMNL). Two sets of homogenic strains, constructed to express either, both, or none of the globotetraosylceramide-sensitive (GS) adhesins specific for globoseries glycolipid receptors or the mannose-sensitive (MS) adhesins inhibited by a-methyl mannoside were compared regarding charge, hydrophobicity, and binding to PMNL. The mutants of a hydrophilic pyelonephritis strain required MS adhesins for binding to and activation of the PMNL. Removal of the MS adhesins from the mutant carrying both MS and GS adhesins abolished chemiluminescence and binding. A pronounced chemiluminescence reaction was induced by the hydrophobic strain without GS or MS adhesins. Transformants of this strain expressing the MS adhesin bound to and activated the PMNL. Poor binding and activation were found with mutants and transformants carrying only the GS adhesins. The improved reactivity after coating of the PMNL with the appropriate receptor glycolipid supported the previously reported absence of globoseries glycolipids in those cells as the reason for the refractoriness to bacteria with GS adhesins. The mechanism of binding, which improves epithelial cell adhesion, may prevent binding to PMNL, thus improving the survival of Escherichia coli in the kidney.

Enterococcus faecalis: specific and non-specific interactions with human polymorphonuclear leukocytes

“…These lectins were also found in the membrane of mouse and human macrophages [8,9], demonstrating that they are widely distributed among phagocytes of different types and sources. The fact that phagocyte/bacterial interactions could be mediated by bacterial lectins and phagocytic sugar containing receptors is a well-known phenomen [4,7,10,11], but the present report stresses the possibility that these interactions could also be mediated by phagocyte lectins and bacterial sugar containing receptors [7]. These mechanisms may also represent an efficient defense mechanism by the host in the absence of opsonins.…”

Bacterial lectins, cell‐cell recognition and infectious disease

“…However, experimental infection by both types of bacteria can be blocked by inhibitory sugars as well as by anti-fimbrial antibodies. Although type P fimbriated E. coli bind poorly to human polymorphonuclear leukocytes, since these cells are deficient in the appropriate receptors, binding is markedly increased if the cells are first coated with globotetraosylceramide (GalNA@3Gala4Gal,84-Glc@Cer) and binding of the bacteria to the coated cells results in metabolic activation [55]. Thus, type P fimbriated E. coli are susceptible to lectinophagocytosis, as are the type 1 fimbriated bacteria.…”

F1651fimbriae of the P fimbrial family inhibit the oxidative response of porcine neutrophils

“…Wild‐type E. coli strain 5131 was isolated from the intestinal contents of a diarrheic and septicemic piglet at the Faculté de Médecine Vétérinaire, Université de Montréal, Saint‐Hyacinthe, Que., Canada. This strain is serum‐resistant, induces septicemia in experimentally inoculated piglets, and is resistant to phagocytic killing by pPMNLs [2–16]. Strain HB101 (pCJ7) is a transformant from plasmid pACYC184 in which was inserted a 10‐kb fragment of DNA (from an F165 1 ‐positive wild‐type septicemia‐inducing E. coli strain 4787) into the Bam HI site [15].…”

“…Mannose‐resistant (MR) non‐fimbrial adhesin 1 (NFA‐1), and P and S fimbriae may induce adhesion of bacteria to hPMNLs. This interaction results in ingestion of bacteria and stimulation of the phagocyte oxidative response, leading to bacterial killing [11,12]. P fimbriae expressing class I PapG adhesin with specificity for the Gal‐Gal moiety prevent attachment of bacteria to human neutrophils, thus protecting cells from phagocyte bacterial activity [13].…”