Identification of the specific oligosaccharide sites recognized by type 1 fimbriae from Escherichia coli on nonspecific cross-reacting antigen, a CD66 cluster granulocyte glycoprotein

• Published in: The Journal of biological chemistry Vol. 268; no. 21; pp. 15510 - 15516
• Main Authors: SAUTER, S. L, RUTHERFURD, S. M, WAGENER, C, SHIVELY, J. E, HEFTA, S. A
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 25-07-1993
• Subjects: Amino Acid Sequence; Antigenic determinants, haptens, artificial antigens; Antigens; Antigens, CD - chemistry; Antigens, CD - metabolism; Antigens, Differentiation - chemistry; Antigens, Differentiation - metabolism; Antigens, Neoplasm; Base Sequence; Binding Sites; Biological and medical sciences; Blotting, Western; Cell Adhesion Molecules; Cloning, Molecular; Cross Reactions; DNA; Escherichia coli; Escherichia coli - metabolism; Fimbriae, Bacterial - metabolism; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Glycosylation; HeLa Cells; Humans; Lectins; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - metabolism; Molecular immunology; Molecular Sequence Data; Oligosaccharides - chemistry; Oligosaccharides - metabolism; Transfection; Tumor Cells, Cultured; Escherichia coli; Oligosaccharide; Granulocyte; Bacteria; Cell cell interaction; Glycoproteins; Binding site; Fimbria; Enterobacteriaceae
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(18)82286-4

Nonspecific cross-reacting antigen (NCA), a CD66 cluster antigen, is a well characterized glycoprotein on granulocytes, macrophages,
and lung epithelium. Structural studies at the protein and genomic levels have revealed that NCA is a member of the immunoglobulin
(Ig) supergene family and contains a domain structure similar to Ig with an amino-terminal variable-like domain followed by
disulfide loop-containing constant-like domains. Previous work by this laboratory and others has demonstrated that NCA is
a receptor for binding of bacteria expressing type 1 fimbriae (pili). This binding is mediated by interaction between lectins
on the bacteria fimbriae and carbohydrate chains on NCA. In the present work we further characterize the specificity for bacterial
binding by NCA using endoglycosidases and site-directed mutagenesis. Results of these studies demonstrate that Escherichia
coli expressing type 1 fimbriae binds to high mannose oligosaccharide structures on NCA and that the functionally relevant
sites are located in the variable-like domain of NCA.