Literature DB >> 11042452

Chaperone-assisted pilus assembly and bacterial attachment.

F G Sauer1, M Barnhart, D Choudhury, S D Knight, G Waksman, S J Hultgren.   

Abstract

Bacterial pili assembled by the chaperone-usher pathway can mediate microbial attachment, an early step in the establishment of an infection, by binding specifically to sugars present in host tissues. Recent work has begun to reveal the structural basis both of chaperone function in the biogenesis of these pili and of bacterial attachment.

Entities:  

Mesh:

Substances:

Year:  2000        PMID: 11042452     DOI: 10.1016/s0959-440x(00)00129-9

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  34 in total

1.  Characterization of FasG segments required for 987P fimbria-mediated binding to piglet glycoprotein receptors.

Authors:  B K Choi; D M Schifferli
Journal:  Infect Immun       Date:  2001-11       Impact factor: 3.441

2.  Chaperone-subunit-usher interactions required for donor strand exchange during bacterial pilus assembly.

Authors:  Michelle M Barnhart; Frederic G Sauer; Jerome S Pinkner; Scott J Hultgren
Journal:  J Bacteriol       Date:  2003-05       Impact factor: 3.490

3.  The type IV pilus assembly complex: biogenic interactions among the bundle-forming pilus proteins of enteropathogenic Escherichia coli.

Authors:  Sandra W Ramer; Gary K Schoolnik; Cheng-Yen Wu; Jaiweon Hwang; Sarah A Schmidt; David Bieber
Journal:  J Bacteriol       Date:  2002-07       Impact factor: 3.490

4.  A cross-genomic approach for systematic mapping of phenotypic traits to genes.

Authors:  Kam Jim; Kush Parmar; Mona Singh; Saeed Tavazoie
Journal:  Genome Res       Date:  2004-01       Impact factor: 9.043

5.  Signal sequence mutations as tools for the characterization of LamB folding intermediates.

Authors:  Amy Rizzitello Duguay; Thomas J Silhavy
Journal:  J Bacteriol       Date:  2002-12       Impact factor: 3.490

6.  Fast uncoiling kinetics of F1C pili expressed by uropathogenic Escherichia coli are revealed on a single pilus level using force-measuring optical tweezers.

Authors:  Mickaël Castelain; Sarah Ehlers; Jeanna Klinth; Stina Lindberg; Magnus Andersson; Bernt Eric Uhlin; Ove Axner
Journal:  Eur Biophys J       Date:  2010-12-16       Impact factor: 1.733

7.  Catalysis of protein folding by chaperones in pathogenic bacteria.

Authors:  James G Bann; Jerome S Pinkner; Carl Frieden; Scott J Hultgren
Journal:  Proc Natl Acad Sci U S A       Date:  2004-12-06       Impact factor: 11.205

8.  The unfolding of the P pili quaternary structure by stretching is reversible, not plastic.

Authors:  Erik Fällman; Staffan Schedin; Jana Jass; Bernt-Eric Uhlin; Ove Axner
Journal:  EMBO Rep       Date:  2005-01       Impact factor: 8.807

9.  Nanoscale characterization and determination of adhesion forces of Pseudomonas aeruginosa pili by using atomic force microscopy.

Authors:  Ahmed Touhami; Manfred H Jericho; Jessica M Boyd; Terry J Beveridge
Journal:  J Bacteriol       Date:  2006-01       Impact factor: 3.490

10.  Resolving the energy paradox of chaperone/usher-mediated fibre assembly.

Authors:  Anton V Zavialov; Vladimir M Tischenko; Laura J Fooks; Bjørn O Brandsdal; Johan Aqvist; Vladimir P Zav'yalov; Sheila Macintyre; Stefan D Knight
Journal:  Biochem J       Date:  2005-08-01       Impact factor: 3.857

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.