Neutrophil-Activating Protein Mediates Adhesion of Helicobacter pylori to Sulfated Carbohydrates on High-Molecular-Weight Salivary Mucin
AUTOR(ES)
Namavar, Ferry
FONTE
American Society for Microbiology
RESUMO
The in vitro binding of surface-exposed material and outer membrane proteins of Helicobacter pylori to high-molecular-weight salivary mucin was studied. We identified a 16-kDa surface protein which adhered to high-molecular-weight salivary mucin. This protein binds specifically to sulfated oligosaccharide structures such as sulfo-Lewis a, sulfogalactose and sulfo-N-acetyl-glucosamine on mucin. Sequence analysis of the protein proved that it was identical to the N-terminal amino acid sequence of neutrophil-activating protein. Moreover, this adhesin was able to bind to Lewis x blood group antigen.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=107925Documentos Relacionados
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