A role for amyloid in cell aggregation and biofilm formation.
A role for amyloid in cell aggregation and biofilm formation.
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DOI:
10.1371/journal.pone.0017632
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发表时间:
2011-03-08
期刊:
影响因子:
3.7
通讯作者:
Lipke PN
中科院分区:
文献类型:
--
作者:
Garcia MC;Lee JT;Ramsook CB;Alsteens D;Dufrêne YF;Lipke PN
Cell adhesion molecules in Saccharomyces cerevisiae and Candida albicans contain amyloid-forming sequences that are highly conserved. We have now used site-specific mutagenesis and specific peptide perturbants to explore amyloid-dependent activity in the Candida albicans adhesin Als5p. A V326N substitution in the amyloid-forming region conserved secondary structure and ligand binding, but abrogated formation of amyloid fibrils in soluble Als5p and reduced cell surface thioflavin T fluorescence. When displayed on the cell surface, Als5p with this substitution prevented formation of adhesion nanodomains and formation of large cellular aggregates and model biofilms. In addition, amyloid nanodomains were regulated by exogenous peptides. An amyloid-forming homologous peptide rescued aggregation and biofilm activity of Als5pV326N cells, and V326N substitution peptide inhibited aggregation and biofilm activity in Als5pWT cells. Therefore, specific site mutation, inhibition by anti-amyloid peturbants, and sequence-specificity of pro-amyloid and anti-amyloid peptides showed that amyloid formation is essential for nanodomain formation and activation.
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影响因子:
--
作者:
Gaur, NK;Smith, RL;Klotz, SA
通讯作者:
Klotz, SA
影响因子:
2.6
作者:
Gonzalez, Marlyn;Goddard, Noel;Hicks, Charles;Ovalle, Rafael;Rauceo, Jason M.;Jue, Chong K.;Lipke, Peter N.
通讯作者:
Lipke, Peter N.
影响因子:
3.6
作者:
de Jong, Wouter;Wosten, Han A. B.;Claessen, Dennis
通讯作者:
Claessen, Dennis
DOI:
10.1073/pnas.96.7.3590
发表时间:
1999-03-30
影响因子:
11.1
作者:
Chiti, F;Webster, P;Dobson, CM
通讯作者:
Dobson, CM
影响因子:
7.6
作者:
Chandra, J;Mukherjee, PK;Ghannoum, MA
通讯作者:
Ghannoum, MA