HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Vretou, E. Articles by Psarrou, E. Search for Related Content PubMed PubMed Citation Articles by Vretou, E. Articles by Psarrou, E. Agricola Articles by Vretou, E. Articles by Psarrou, E.

Polymorphic outer-membrane proteins of Chlamydophila abortus are glycosylated

Department of Microbiology, Hellenic Pasteur Institute, Vassilissis Sofias 127, Athens 11521, Greece¹

Author for correspondence: Evangelia Vretou. Tel: +30 1 64 78 873. Fax: +30 1 64 78 873. e-mail: vretou{at}mail.pasteur.gr

Antigenic profiles of mono-, bi- and poly-specific monoclonal antibodies against 90 kDa polymorphic outer-membrane proteins (POMPs) and a 105 kDa POMP-related protein of Chlamydophila abortus ATCC VR 656^T, after one- and two-dimensional electrophoretic analysis, helped identify each one of the triplets POMP 90, 91A and 91B, and a POMP-related protein at 85 kDa. The lectin concanavalin A bound to the four POMPs and the POMP-related protein in a specific manner and the binding was sensitive to treatment with the amidase N-endoglycosidase F, suggesting the presence of small asparagine-linked oligosaccharide chains. The exposure of the five proteins on the chlamydial surface and the orientation of the attached oligosaccharide chains was examined by protease and endoglycosidase treatments of intact bacteria. The results were consistent with the concept that some of the oligosaccharides in the POMPs face outwards, possibly protecting the polypeptides from proteolytic enzymes, whereas the oligosaccharides in the 105 kDa POMP-related protein are oriented inwards, thereby rendering the polypeptide chain accessible to proteases. A possible role for the N-linked oligosaccharides in the POMPs might be the promotion of the proper folding and processing of these proteins.

Keywords: polymorphic outer-membrane protein family, bacterial glycoprotein, concanavalin A, two-dimensional electrophoresis

Abbreviations: ConA, concanavalin A; EB, elementary body; MOMP, major outer-membrane protein; OG, n-octyl ß-D-glucopyranoside; OMC, outer-membrane complex; PMP, polymorphic membrane protein; PNGase F, N-endoglycosidase F from Flavobacterium meningosepticum; POMP, polymorphic outer-membrane protein

This article has been cited by other articles:

				I. R. Henderson, F. Navarro-Garcia, M. Desvaux, R. C. Fernandez, and D. Ala'Aldeen Type V Protein Secretion Pathway: the Autotransporter Story Microbiol. Mol. Biol. Rev., December 1, 2004; 68(4): 692 - 744. [Abstract] [Full Text] [PDF]

				E. Vretou, P. Giannikopoulou, D. Longbottom, and E. Psarrou Antigenic Organization of the N-Terminal Part of the Polymorphic Outer Membrane Proteins 90, 91A, and 91B of Chlamydophilaabortus Infect. Immun., June 1, 2003; 71(6): 3240 - 3250. [Abstract] [Full Text] [PDF]