Document Detail


The HMW1 adhesin of nontypeable Haemophilus influenzae recognizes sialylated glycoprotein receptors on cultured human epithelial cells.
MedLine Citation:
PMID:  8063405     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Disease due to nontypeable Haemophilus influenzae begins with colonization of the upper respiratory tract mucosa. We recently reported that two surface-exposed high-molecular-weight proteins (HMW1 and HMW2) expressed by a prototypic strain of nontypeable H. influenzae mediate attachment to cultured epithelial cells. In the present study, we examined the nature of the epithelial cell receptor with which HMW1 interacts. Both proteinase K pretreatment and periodate oxidation of epithelial monolayers resulted in a marked decrease in HMW1-mediated binding, suggesting interaction with a glycoprotein structure. Treatment with peptide-N-glycosidase F produced a similar decrease in attachment and thereby provided further evidence for this conclusion. Desialylation of the epithelial cell surface also reduced binding, implying the presence of sialic acid in the receptor structure. Furthermore, lectins specific for terminal alpha 2-3-linked sialic acid were capable of inhibiting HMW1-mediated attachment. In summary, our results indicate that the HMW1 adhesin interacts with a glycoprotein receptor containing N-linked oligosaccharide chains with sialic acid in an alpha 2-3 configuration.
Authors:
J W St Geme
Related Documents :
7599985 - Isolation, purification and characterization of porcine serum transferrin and hemopexin.
239685 - The sialic acid content and isoelectric point of human kininogen.
12135555 - High-level expression of recombinant neisseria cmp-sialic acid synthetase in escherichi...
8164395 - The relationship between the sialic acid concentrations in the serum and whole saliva i...
15560075 - Simple and rapid procedure suitable for quantitative isolation of low and high molecula...
16614985 - Increased antioxidant capacity of serum did not prevent lipid peroxidation in the inter...
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Infection and immunity     Volume:  62     ISSN:  0019-9567     ISO Abbreviation:  Infect. Immun.     Publication Date:  1994 Sep 
Date Detail:
Created Date:  1994-09-21     Completed Date:  1994-09-21     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0246127     Medline TA:  Infect Immun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3881-9     Citation Subset:  IM    
Affiliation:
Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, St. Louis, Missouri 63110.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Bacterial Adhesion*
Bacterial Proteins / metabolism*
Cells, Cultured
Epithelium / metabolism
Haemophilus influenzae / metabolism*
Humans
Membrane Glycoproteins / analysis*
N-Acetylneuraminic Acid
Neuraminidase / pharmacology
Receptors, Cell Surface / analysis*
Sialic Acids / analysis*
Grant Support
ID/Acronym/Agency:
HD-29678/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Membrane Glycoproteins; 0/Receptors, Cell Surface; 0/Sialic Acids; 131-48-6/N-Acetylneuraminic Acid; EC 3.2.1.18/Neuraminidase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Variable region sequences of a protective human monoclonal antibody specific for the Haemophilus inf...
Next Document:  Differential flagellin expression in a flaA flaB+ mutant of Campylobacter jejuni.