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The major subunit, CfaB, of colonization factor antigen i from enterotoxigenic Escherichia coli is a glycosphingolipid binding protein.

Artikel i vetenskaplig tidskrift
Författare Lena Jansson
Joshua Tobias
Michael Lebens
Ann-Mari Svennerholm
Susann Teneberg
Publicerad i Infection and immunity
Volym 74
Nummer/häfte 6
Sidor 3488-97
ISSN 0019-9567
Publiceringsår 2006
Publicerad vid Institutionen för biomedicin, avdelningen för mikrobiologi och immunologi
Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 3488-97
Språk en
Länkar dx.doi.org/10.1128/IAI.02006-05
Ämnesord Carrier Proteins, metabolism, Escherichia coli Proteins, metabolism, Fimbriae Proteins, chemistry, metabolism, Fimbriae, Bacterial, Glycosphingolipids, metabolism, Humans, Protein Subunits
Ämneskategorier Mikrobiologi inom det medicinska området

Sammanfattning

Bacterial adherence to mucosal surfaces is an important virulence trait of pathogenic bacteria. Adhesion of enterotoxigenic Escherichia coli (ETEC) to the intestine is mediated by a number of antigenically distinct colonization factors (CFs). One of the most common CFs is CFA/I. This has a fimbrial structure composed of a major repeating subunit, CfaB, and a single tip subunit, CfaE. The potential carbohydrate recognition by CFA/I was investigated by binding CFA/I-fimbriated bacteria and purified CFA/I fimbriae to a large number of variant glycosphingolipids separated on thin-layer chromatograms. For both fimbriated bacteria and purified fimbriae, specific interactions could be identified with a number of nonacid glycosphingolipids. These included glucosylceramide, lactosylceramide with phytosphingosine and/or hydroxy fatty acids, neolactotetraosylceramide, gangliotriaosylceramide, gangliotetraosylceramide, the H5 type 2 pentaglycosylceramide, the Lea-5 glycosphingolipid, the Lex-5 glycosphingolipid, and the Ley-6 glycosphingolipid. These glycosphingolipids were also recognized by recombinant E. coli expressing CFA/I in the absence of tip protein CfaE, as well as by purified fimbriae from the same strain. This demonstrates that the glycosphingolipid-binding capacity of CFA/I resides in the major CfaB subunit.

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