title: Carbohydrate-dependent inhibition of Helicobacter pylori colonization using porcine milk.
abstract: Breast milk has a well-known anti-microbial effect, which is in part due to the many different carbohydrate structures expressed. This renders it a position as a potential therapeutic for treatment of infection by different pathogens, thus avoiding the drawbacks of many antibiotics. In a previous study, we showed that pigs express the Helicobacter pylori receptors, sialyl Lewis x (Le x) and Le b, on various milk proteins. Here, we investigate the pig breed- and individual-specific expression of these epitopes, as well as the inhibitory capacity of porcine milk on H. pylori binding and colonization. Milk proteins from three different pig breeds were analysed by western blotting using antibodies with known carbohydrate specificity. An adhesion assay was used to investigate the capacity of pig milk to inhibit H. pylori binding to neoglycoproteins carrying Le b and sialyl-di-Le x. alpha1,3/4-fucosyltransferase transgenic FVB/N mice, known to express Le b and sialyl Le x in their gastric epithelium, were colonized by H. pylori and were subsequently treated with Le b- and sialyl Le x-expressing or nonexpressing porcine milk, or water (control) only. The degree of H. pylori colonization in the different treatment groups was quantified. The expression of the Le b and sialyl Le x carbohydrate epitopes on pig milk proteins was breed- and individual specific and correlated to the ability of porcine milk to inhibit H. pylori adhesion in vitro and H. pylori colonization in vivo. Milk from certain pig breeds may have a therapeutic and/or prophylactic effect on H. pylori infection.
authors.affiliation: Department of Surgery, Sahlgrenska University Hospital, S-413 45 Göteborg, Sweden. anki.gustafsson@clinchem.gu.se
authors.forename: Anki
authors.initials: A
authors.lastname: Gustafsson
authors.forename: Anna
authors.initials: A
authors.lastname: Hultberg
authors.forename: Rolf
authors.initials: R
authors.lastname: Sjöström
authors.forename: Imre
authors.initials: I
authors.lastname: Kacskovics
authors.forename: Michael E
authors.initials: ME
authors.lastname: Breimer
authors.forename: Thomas
authors.initials: T
authors.lastname: Borén
authors.forename: Lennart
authors.initials: L
authors.lastname: Hammarström
authors.forename: Jan
authors.initials: J
authors.lastname: Holgersson
mesh_terms: D000818:Animals; D001422:Bacterial Adhesion / Q000187:drug effects* / Q000502:physiology; D002241:Carbohydrates / Q000737:chemistry* / Q000235:genetics; D005647:Fucosyltransferases / Q000235:genetics / Q000378:metabolism; D016481:Helicobacter Infections / Q000235:genetics / Q000378:metabolism; D016480:Helicobacter pylori / Q000254:growth & development*; D007983:Lewis Blood Group Antigens / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D051379:Mice; D008822:Mice, Transgenic; D008892:Milk / Q000737:chemistry* / Q000378:metabolism; D008894:Milk Proteins / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D013045:Species Specificity; D013552:Swine
chemical_list: D002241:Carbohydrates; D007983:Lewis Blood Group Antigens; D008894:Milk Proteins; D005647:Fucosyltransferases; C019818:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase