Mikhail V Belousov, Anastasiia O Kosolapova, Haidar Fayoud, Maksim I Sulatsky, Anna I Sulatskaya, Maria N Romanenko, Alexander G Bobylev, Kirill S Antonets, Anton A Nizhnikov
Outer membrane proteins (Omps) of Gram-negative bacteria represent porins involved in a wide range of virulence- and pathogenesis-related cellular processes, including transport, adhesion, penetration, and the colonization of host tissues. Most outer membrane porins share a specific spatial structure called the β-barrel that provides their structural integrity within the membrane lipid bilayer. Recent data suggest that outer membrane proteins from several bacterial species are able to adopt the amyloid state alternative to their β-barrel structure. Amyloids are protein fibrils with a specific spatial structure called the cross-β that gives them an unusual resistance to different physicochemical influences. Various bacterial amyloids are known to be involved in host-pathogen and host-symbiont interactions and contribute to colonization of host tissues. Such an ability of outer membrane porins to adopt amyloid state might represent an important mechanism of bacterial virulence. In this work, we investigated the amyloid properties of the OmpC and OmpF porins from two species belonging to family, , and We demonstrated that OmpC and OmpF of and form toxic fibrillar aggregates in vitro. These aggregates exhibit birefringence upon binding Congo Red dye and show characteristic reflections under X-ray diffraction. Thus, we confirmed amyloid properties for OmpC of and demonstrated amyloid properties for three novel proteins: OmpC of and OmpF of and in vitro. All four studied porins were shown to form amyloid fibrils at the surface of cells in the curli-dependent amyloid generator system. Moreover, we found that overexpression of recombinant OmpC and OmpF in the BL21 strain leads to the formation of detergent- and protease-resistant amyloid-like aggregates and enhances the birefringence of bacterial cultures stained with Congo Red. We also detected detergent- and protease-resistant aggregates comprising OmpC and OmpF in culture. These data are important in the context of understanding the structural dualism of Omps and its relation to pathogenesis.
J Biol Chem. 1989 Oct 25;264(30):17961-70
[PMID:
2478539]
Nat Struct Biol. 2003 Jun;10(6):461-7
[PMID:
12754496]
Cold Spring Harb Protoc. 2018 Jun 1;2018(6):
[PMID:
29858338]
Proteins. 2008 Feb 1;70(2):450-61
[PMID:
17680697]
Food Funct. 2021 Jun 21;12(12):5465-5477
[PMID:
33997868]
J Mol Microbiol Biotechnol. 2002 Jan;4(1):1-10
[PMID:
11763966]
PLoS Biol. 2020 Jul 23;18(7):e3000564
[PMID:
32701952]
Biochemistry (Mosc). 2015 Sep;80(9):1127-44
[PMID:
26555466]
Mol Microbiol. 2000 Jul;37(2):239-53
[PMID:
10931321]
Front Microbiol. 2020 Mar 20;11:397
[PMID:
32265863]
Sci Rep. 2018 Jul 9;8(1):10353
[PMID:
29985420]
Microbiology (Reading). 1997 Aug;143 ( Pt 8):2797-2806
[PMID:
9274033]
Biochemistry (Mosc). 2016 Jan;81(1):34-46
[PMID:
26885581]
Nat Protoc. 2013;8(7):1381-90
[PMID:
23787895]
Science. 1982 Dec 24;218(4579):1309-11
[PMID:
6815801]
Microb Pathog. 2017 Jun;107:29-37
[PMID:
28315387]
PLoS One. 2012;7(2):e30724
[PMID:
22383971]
Mol Gen Genet. 1986 Oct;205(1):51-5
[PMID:
3540530]
Biochim Biophys Acta Biomembr. 2022 Sep 1;1864(9):183971
[PMID:
35643329]
Nature. 1992 Aug 27;358(6389):727-33
[PMID:
1380671]
Int J Mol Sci. 2018 Sep 14;19(9):
[PMID:
30223436]
Biophys J. 2009 Jun 17;96(12):5013-9
[PMID:
19527661]
Science. 1997 Sep 5;277(5331):1453-62
[PMID:
9278503]
Data Brief. 2016 May 20;8:108-13
[PMID:
27294177]
J Bacteriol. 1985 May;162(2):722-7
[PMID:
2580824]
J Biol Chem. 2009 Dec 4;284(49):34382-9
[PMID:
19805550]
Infect Immun. 1984 May;44(2):409-20
[PMID:
6370866]
Protein Eng Des Sel. 2011 Sep;24(9):743-50
[PMID:
21565831]
Int J Mol Sci. 2022 Nov 23;23(23):
[PMID:
36498920]
Mol Gen Genet. 1987 Jul;208(3):511-7
[PMID:
2823064]
Front Plant Sci. 2022 Oct 24;13:1014699
[PMID:
36388578]
Methods Enzymol. 1999;309:649-73
[PMID:
10507053]
Int J Mol Sci. 2020 Sep 30;21(19):
[PMID:
33008049]
Trends Genet. 2000 Jun;16(6):276-7
[PMID:
10827456]
PLoS One. 2012;7(5):e36969
[PMID:
22590640]
PLoS One. 2010 Jul 14;5(7):e11517
[PMID:
20644720]
Int J Mol Sci. 2018 May 03;19(5):
[PMID:
29751510]
J Cell Biol. 1980 Jul;86(1):327-9
[PMID:
6252213]
Science. 1982 Mar 5;215(4537):1243-5
[PMID:
6120571]
FEBS Lett. 1992 Jul 20;306(2-3):251-6
[PMID:
1633882]
RSC Adv. 2021 Mar 17;11(19):11192-11203
[PMID:
35423661]
J Mol Biol. 1997 Oct 31;273(3):729-39
[PMID:
9356260]
Microorganisms. 2023 Jun 28;11(7):
[PMID:
37512863]
Langmuir. 2018 May 15;34(19):5623-5634
[PMID:
29166022]
J Bacteriol. 1983 Jan;153(1):241-52
[PMID:
6294049]
J Biol Chem. 1983 Jun 10;258(11):6932-40
[PMID:
6304064]
Nature. 2021 Aug;596(7873):583-589
[PMID:
34265844]
J Virol. 2017 Sep 12;91(19):
[PMID:
28701406]
Membranes (Basel). 2022 Oct 10;12(10):
[PMID:
36295740]
PLoS One. 2014 Jul 29;9(7):e103878
[PMID:
25072376]
Genes Dev. 2012 Dec 1;26(23):2659-67
[PMID:
23166018]
Evol Bioinform Online. 2018 Apr 09;14:1176934318768781
[PMID:
29720870]
Vet Microbiol. 2013 May 3;163(3-4):207-22
[PMID:
22986056]
J Biol Chem. 2003 May 16;278(20):17701-9
[PMID:
12584201]
Microbiology (Reading). 2006 Feb;152(Pt 2):485-491
[PMID:
16436436]
Annu Rev Biochem. 1998;67:509-44
[PMID:
9759496]
Antonie Van Leeuwenhoek. 2018 Dec;111(12):2311-2321
[PMID:
29974354]
Philos Trans R Soc Lond B Biol Sci. 2015 Oct 5;370(1679):
[PMID:
26370935]
Infect Immun. 1991 Jan;59(1):449-52
[PMID:
1846127]
PLoS One. 2015 Jul 21;10(7):e0132301
[PMID:
26196893]
Arch Biochem Biophys. 2013 Mar;531(1-2):34-43
[PMID:
23131493]
J Mol Biol. 1981 Mar 25;147(1):195-7
[PMID:
7265238]
Prog Mol Biol Transl Sci. 2021;183:75-99
[PMID:
34656335]
Cold Spring Harb Perspect Biol. 2019 Dec 2;11(12):
[PMID:
31088827]
Amyloid. 2022 Dec;29(4):213-219
[PMID:
36420821]
Int J Mol Sci. 2021 Oct 20;22(21):
[PMID:
34768745]
J Med Chem. 2008 May 22;51(10):2871-8
[PMID:
18260614]
Proc Natl Acad Sci U S A. 2007 Oct 30;104(44):17388-93
[PMID:
17959784]
Int J Mol Sci. 2018 Aug 23;19(9):
[PMID:
30142878]
Biotechnol Lett. 2016 Apr;38(4):689-700
[PMID:
26712371]
Int J Biol Macromol. 2021 Dec 1;192:1304-1310
[PMID:
34687761]
J Virol. 2019 Sep 30;93(20):
[PMID:
31142669]
Protein Sci. 2007 Apr;16(4):744-54
[PMID:
17384235]
PLoS One. 2013;8(1):e54175
[PMID:
23326595]
J Biol Chem. 2006 Jun 23;281(25):17114-17123
[PMID:
16618701]
Micron. 2009 Apr;40(3):285-301
[PMID:
19019688]
Anal Biochem. 1989 Mar;177(2):244-9
[PMID:
2729542]
Can J Microbiol. 1999 Aug;45(8):658-69
[PMID:
10528398]
Methods Mol Biol. 2012;849:303-20
[PMID:
22528099]
Lett Appl Microbiol. 2006 Mar;42(3):195-201
[PMID:
16478504]
Nucleic Acids Res. 2018 Jul 2;46(W1):W315-W322
[PMID:
29893907]
Biomolecules. 2019 Nov 04;9(11):
[PMID:
31690032]
Proc Natl Acad Sci U S A. 1978 Aug;75(8):3751-5
[PMID:
358202]
