Autotransporter Proteins: Novel Targets at the Bacterial Cell Surface

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Title Autotransporter Proteins: Novel Targets at the Bacterial Cell Surface
Author Wells, Timothy J.; Tree, Jai J.; Ulett, Glen Charles; Schembri, Mark A.
Publication Title FEMS Microbiology Letters
Year Published 2007
Place of publication The Netherlands
Publisher Elsevier Science B.V. for The Federation of European Microbiological Societies
Abstract Autotransporter proteins constitute a family of outer membrane/secreted proteins that possess unique structural properties that facilitate their independent transport across the bacterial membrane system and final routing to the cell surface. Autotransporter proteins have been identified in a wide range of Gram-negative bacteria and are often associated with virulence functions such as adhesion, aggregation, invasion, biofilm formation and toxicity. The importance of autotransporter proteins is exemplified by the fact that they constitute an essential component of some human vaccines. Autotransporter proteins contain three structural motifs: a signal sequence, a passenger domain and a translocator domain. Here, the structural properties of the passenger and translocator domains of three type Va autotransporter proteins are compared and contrasted, namely pertactin from Bordetella pertussis, the adhesion and penetration protein (Hap) from Haemophilus influenzae and Antigen 43 (Ag43) from Escherichia coli. The Ag43 protein is described in detail to examine how its structure relates to functional properties such as cell adhesion, aggregation and biofilm formation. The widespread occurrence of autotransporter-encoding genes, their apparent uniform role in virulence and their ability to interact with host cells suggest that they may represent rational targets for the design of novel vaccines directed against Gram-negative pathogens.
Peer Reviewed No
Published Yes
Alternative URI http://dx.doi.org/10.1111/j.1574-6968.2007.00833.x
Volume 274
Issue Number 2
Page from 163
Page to 172
ISBN or ISSN 0378-1097
Date Accessioned 2009-02-20; 2012-05-10T22:36:12Z
Date Available 2012-05-10T22:36:12Z
Research Centre Griffith Health Institute; Molecular Basis of Disease
Faculty Griffith Health Faculty
Subject Medical Bacteriology
URI http://hdl.handle.net/10072/45043
Publication Type Major Reviews/Reports
Publication Type Code dx

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