REVIEW

Cell surface amyloid proteins of microorganisms: structure, properties and significance in medicine

Rekstina VV1, Gorkovskii AA2, Bezsonov EE2, Kalebina TS1
About authors

1 Faculty of Biology, Department of Molecular Biology,
Lomonosov Moscow State University, Moscow, Russia

2 Laboratory of Biochemistry and Genetics,
National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA

Correspondence should be addressed: Tatiana Kalebina
Leninskie gory, d. 2, str. 12, Moscow, Russia, 119899; ur.usm.eebeneg@anibelak

About paper

Funding: this study was supported by the Russian Foundation for Basic Research (grant no. 14-04-01187 A).

Received: 2015-09-30 Accepted: 2015-10-07 Published online: 2017-01-05
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This review summarizes data which describe properties of microbial cell surface amyloids proteins. Definitions of amyloids and microbial functional amyloids are given. The review provides numerous examples of research in which the presence of amyloid-like properties in microbial cell surface proteins is demonstrated convincingly. Studies of the important role of pili, curli, tafi and some other bacterial fibrillar proteins in host colonization are reviewed. Data on amyloid proteins of yeast cell surface, their properties and potential association with candidiasis development are summarized. This review also appeals to experts in biology and medicine in an attempt to draw their attention to the issue which is increasingly discussed in scientific work at present, namely to a possible role of bacterial extracellular matrix amyloids and amyloid proteins of eukaryotic microorganism surface, yeast in the first place, in the development of amyloidosis in animals and humans.

Keywords: microbial cell surface, microbial amyloid, functional amyloid, pili, curli, tafi, phenol soluble modulin, adhesin, class I hydrophobin, amyloidosis

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