DSB proteins and bacterial pathogenicity-Reference-Cited by-同舟云学术

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DSB proteins and bacterial pathogenicity

Published:2009-02-09 Issue:3 Volume:7 Page:215-225
ISSN:1740-1526
Container-title:Nature Reviews Microbiology
language:en
Short-container-title:Nat Rev Microbiol

Author:

Heras Begoña,Shouldice Stephen R.,Totsika Makrina,Scanlon Martin J.,Schembri Mark A.,Martin Jennifer L.

Publisher

Springer Science and Business Media LLC

Subject

General Immunology and Microbiology,Microbiology,Infectious Diseases

Link

http://www.nature.com/articles/nrmicro2087.pdf

Reference100 articles.

1. Heras, B., Kurz, M., Shouldice, S. R. & Martin, J. L. The name's bond......disulfide bond. Curr. Opin. Struct. Biol. 17, 691–698 (2007).

2. Lee, Y. M., Almqvist, F. & Hultgren, S. J. Targeting virulence for antimicrobial chemotherapy. Curr. Opin. Pharmacol. 3, 513–519 (2003).

3. Dutton, R. J., Boyd, D., Berkmen, M. & Beckwith, J. Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc. Natl Acad. Sci. USA 105, 11933–11938 (2008). This thorough study combines bioinformatic and experimental data to show the great diversity of the disulphide machinery throughout the bacterial kingdom.

4. Jacob-Dubuisson, F. et al. PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA. Proc. Natl Acad. Sci. USA 91, 11552–11556 (1994). This paper shows that DsbA catalyses the correct folding of the fimbrial chaperone PapD, ensuring its subsequent complex formation with the fimbrial subunits and PapG adhesin.

5. Stenson, T. H. & Weiss, A. A. DsbA and DsbC are required for secretion of pertussis toxin by Bordetella pertussis. Infect. Immun. 70, 2297–2303 (2002).

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